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Bifunctional cytochrome P450/NADPH--P450 reductase (Cytochrome P450(BM-3)) (Cytochrome P450BM-3) (Fatty acid monooxygenase) (Flavocytochrome P450 BM3) [Includes: Cytochrome P450 102A1 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]

 CPXB_BACMB              Reviewed;        1049 AA.
P14779; A0A0B6AQ66; Q9AE23;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-APR-2018, entry version 155.
RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase {ECO:0000305};
AltName: Full=Cytochrome P450(BM-3) {ECO:0000303|PubMed:15299332};
AltName: Full=Cytochrome P450BM-3 {ECO:0000303|PubMed:8342039, ECO:0000312|EMBL:AAK19020.1};
AltName: Full=Fatty acid monooxygenase {ECO:0000303|PubMed:3106359};
AltName: Full=Flavocytochrome P450 BM3 {ECO:0000303|PubMed:11695889, ECO:0000303|PubMed:14653735};
Includes:
RecName: Full=Cytochrome P450 102A1;
EC=1.14.14.1 {ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081};
Includes:
RecName: Full=NADPH--cytochrome P450 reductase;
EC=1.6.2.4 {ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081};
Name=cyp102A1 {ECO:0000312|EMBL:AJI21949.1}; Synonyms=cyp102;
ORFNames=BG04_163 {ECO:0000312|EMBL:AJI21949.1};
Bacillus megaterium (strain ATCC 14581 / DSM 32 / JCM 2506 / NBRC
15308 / NCIMB 9376 / NCTC 10342 / VKM B-512).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=1348623;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC
10342 / VKM B-512 {ECO:0000303|PubMed:2544578};
PubMed=2544578;
Ruettinger R.T., Wen L.-P., Fulco A.J.;
"Coding nucleotide, 5' regulatory, and deduced amino acid sequences of
P-450BM-3, a single peptide cytochrome P-450:NADPH-P-450 reductase
from Bacillus megaterium.";
J. Biol. Chem. 264:10987-10995(1989).
[2] {ECO:0000312|EMBL:AJI21949.1, ECO:0000312|Proteomes:UP000031829}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC
10342 / VKM B-512 {ECO:0000312|EMBL:AJI21949.1};
PubMed=25931591; DOI=10.1128/genomeA.00151-15;
Johnson S.L., Daligault H.E., Davenport K.W., Jaissle J., Frey K.G.,
Ladner J.T., Broomall S.M., Bishop-Lilly K.A., Bruce D.C.,
Gibbons H.S., Coyne S.R., Lo C.C., Meincke L., Munk A.C.,
Koroleva G.I., Rosenzweig C.N., Palacios G.F., Redden C.L.,
Minogue T.D., Chain P.S.;
"Complete genome sequences for 35 biothreat assay-relevant bacillus
species.";
Genome Announc. 3:0-0(2015).
[3] {ECO:0000312|EMBL:AAK19020.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29, AND INDUCTION.
STRAIN=ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC
10342 / VKM B-512 {ECO:0000303|PubMed:1544926};
PubMed=1544926;
Shaw G.C., Fulco A.J.;
"Barbiturate-mediated regulation of expression of the cytochrome
P450BM-3 gene of Bacillus megaterium by Bm3R1 protein.";
J. Biol. Chem. 267:5515-5526(1992).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
STRAIN=ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC
10342 / VKM B-512 {ECO:0000303|PubMed:3106359};
PubMed=3106359;
Wen L.P., Fulco A.J.;
"Cloning of the gene encoding a catalytically self-sufficient
cytochrome P-450 fatty acid monooxygenase induced by barbiturates in
Bacillus megaterium and its functional expression and regulation in
heterologous (Escherichia coli) and homologous (Bacillus megaterium)
hosts.";
J. Biol. Chem. 262:6676-6682(1987).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
PubMed=1727637; DOI=10.1016/0003-9861(92)90045-X;
Boddupalli S.S., Pramanik B.C., Slaughter C.A., Estabrook R.W.,
Peterson J.A.;
"Fatty acid monooxygenation by P450BM-3: product identification and
proposed mechanisms for the sequential hydroxylation reactions.";
Arch. Biochem. Biophys. 292:20-28(1992).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ALA-75; PHE-88 AND
LEU-189.
PubMed=16566047; DOI=10.1002/cbic.200500444;
Budde M., Morr M., Schmid R.D., Urlacher V.B.;
"Selective hydroxylation of highly branched fatty acids and their
derivatives by CYP102A1 from Bacillus megaterium.";
ChemBioChem 7:789-794(2006).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18020460; DOI=10.1021/bi701945j;
Chowdhary P.K., Keshavan N., Nguyen H.Q., Peterson J.A.,
Gonzalez J.E., Haines D.C.;
"Bacillus megaterium CYP102A1 oxidation of acyl homoserine lactones
and acyl homoserines.";
Biochemistry 46:14429-14437(2007).
[8] {ECO:0000244|PDB:2HPD}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-472 IN COMPLEX WITH HEME.
PubMed=8342039; DOI=10.1126/science.8342039;
Ravichandran K.G., Boddupalli S.S., Hasemann C.A., Peterson J.A.,
Deisenhofer J.;
"Crystal structure of hemoprotein domain of P450BM-3, a prototype for
microsomal P450's.";
Science 261:731-736(1993).
[9] {ECO:0000244|PDB:2BMH}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-456 IN COMPLEX WITH HEME.
PubMed=15299332; DOI=10.1107/S0907444994009194;
Li H., Poulos T.L.;
"Modeling protein-substrate interactions in the heme domain of
cytochrome P450(BM-3).";
Acta Crystallogr. D 51:21-32(1995).
[10] {ECO:0000244|PDB:1FAH}
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-472 OF MUTANT ALA-269 IN
COMPLEX WITH HEME, CATALYTIC ACTIVITY, COFACTOR, SITE, AND MUTAGENESIS
OF THR-269.
PubMed=7578081; DOI=10.1021/bi00045a014;
Yeom H., Sligar S.G., Li H., Poulos T.L., Fulco A.J.;
"The role of Thr268 in oxygen activation of cytochrome P450BM-3.";
Biochemistry 34:14733-14740(1995).
[11] {ECO:0000244|PDB:1FAG}
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-472 IN COMPLEX WITH HEME
AND PALMITOLEIC ACID.
PubMed=9033595; DOI=10.1038/nsb0297-140;
Li H.Y., Poulos T.L.;
"The structure of the cytochrome p450BM-3 haem domain complexed with
the fatty acid substrate, palmitoleic acid.";
Nat. Struct. Biol. 4:140-146(1997).
[12] {ECO:0000244|PDB:1BU7, ECO:0000244|PDB:1BVY}
X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 2-650 IN COMPLEX WITH FMN
AND HEME.
PubMed=10051560; DOI=10.1073/pnas.96.5.1863;
Sevrioukova I.F., Li H., Zhang H., Peterson J.A., Poulos T.L.;
"Structure of a cytochrome P450-redox partner electron-transfer
complex.";
Proc. Natl. Acad. Sci. U.S.A. 96:1863-1868(1999).
[13] {ECO:0000244|PDB:1JME}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-456 OF MUTANT HIS-394 IN
COMPLEX WITH HEME, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-394.
PubMed=11695889; DOI=10.1021/bi010717e;
Ost T.W., Munro A.W., Mowat C.G., Taylor P.R., Pesseguiero A.,
Fulco A.J., Cho A.K., Cheesman M.A., Walkinshaw M.D., Chapman S.K.;
"Structural and spectroscopic analysis of the F393H mutant of
flavocytochrome P450 BM3.";
Biochemistry 40:13430-13438(2001).
[14] {ECO:0000244|PDB:1JPZ}
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-471 IN COMPLEX WITH HEME
AND N-PALMITOYLGLYCINE, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=11695892; DOI=10.1021/bi011197q;
Haines D.C., Tomchick D.R., Machius M., Peterson J.A.;
"Pivotal role of water in the mechanism of P450BM-3.";
Biochemistry 40:13456-13465(2001).
[15] {ECO:0000244|PDB:1P0V, ECO:0000244|PDB:1P0W, ECO:0000244|PDB:1P0X}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-456 OF MUTANTS
ALA/TRP/TYR-394 IN COMPLEXES WITH HEME, FUNCTION, CATALYTIC ACTIVITY,
AND MUTAGENESIS OF PHE-394.
PubMed=14653735; DOI=10.1021/ja035731o;
Ost T.W., Clark J., Mowat C.G., Miles C.S., Walkinshaw M.D.,
Reid G.A., Chapman S.K., Daff S.;
"Oxygen activation and electron transfer in flavocytochrome P450
BM3.";
J. Am. Chem. Soc. 125:15010-15020(2003).
[16] {ECO:0000244|PDB:1SMI, ECO:0000244|PDB:1SMJ}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-472 OF MUTANT GLU-265 IN
COMPLEXES WITH HEME AND PALMITOLEIC ACID.
PubMed=15020590; DOI=10.1074/jbc.M401717200;
Joyce M.G., Girvan H.M., Munro A.W., Leys D.;
"A single mutation in cytochrome P450 BM3 induces the conformational
rearrangement seen upon substrate binding in the wild-type enzyme.";
J. Biol. Chem. 279:23287-23293(2004).
[17] {ECO:0000244|PDB:1YQO, ECO:0000244|PDB:1YQP}
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-456 OF MUTANTS ALA/ASN-269
IN COMPLEXES WITH HEME, CATALYTIC ACTIVITY, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME KINETICS, ABSORPTION
SPECTROSCOPY, REDOX POTENTIOMETRY OF HEME, AND MUTAGENESIS OF THR-269
AND PHE-394.
PubMed=16403573; DOI=10.1016/j.jinorgbio.2005.11.020;
Clark J.P., Miles C.S., Mowat C.G., Walkinshaw M.D., Reid G.A.,
Daff S.N., Chapman S.K.;
"The role of Thr268 and Phe393 in cytochrome P450 BM3.";
J. Inorg. Biochem. 100:1075-1090(2006).
[18] {ECO:0000244|PDB:1ZO9}
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-471 IN COMPLEX WITH HEME
AND N-PALMITOYL-L-METHIONINE, FUNCMTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-48.
PubMed=18004886; DOI=10.1021/bi701667m;
Hegde A., Haines D.C., Bondlela M., Chen B., Schaffer N.,
Tomchick D.R., Machius M., Nguyen H., Chowdhary P.K., Stewart L.,
Lopez C., Peterson J.A.;
"Interactions of substrates at the surface of P450s can greatly
enhance substrate potency.";
Biochemistry 46:14010-14017(2007).
[19] {ECO:0000244|PDB:2J1M, ECO:0000244|PDB:2J4S}
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-456 IN COMPLEXES WITH HEME.
PubMed=17429965; DOI=10.1021/ja067036x;
Kuper J., Wong T.S., Roccatano D., Wilmanns M., Schwaneberg U.;
"Understanding a mechanism of organic cosolvent inactivation in heme
monooxygenase P450 BM-3.";
J. Am. Chem. Soc. 129:5786-5787(2007).
[20] {ECO:0000244|PDB:2IJ2, ECO:0000244|PDB:2IJ3, ECO:0000244|PDB:2IJ4}
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 2-471 OF WILD-TYPE AND
MUTANTS HIS/LYS-265 IN COMPLEXES WITH HEME, FUNCTION, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF ALA-265.
PubMed=17077084; DOI=10.1074/jbc.M607949200;
Girvan H.M., Seward H.E., Toogood H.S., Cheesman M.R., Leys D.,
Munro A.W.;
"Structural and spectroscopic characterization of P450 BM3 mutants
with unprecedented P450 heme iron ligand sets. New heme ligation
states influence conformational equilibria in P450 BM3.";
J. Biol. Chem. 282:564-572(2007).
[21] {ECO:0000244|PDB:2UWH}
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-459 OF MUTANT PHE-83 IN
COMPLEX WITH HEME AND PALMITIC ACID, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME KINETICS, AND MUTAGENESIS OF
ALA-83.
PubMed=17868686; DOI=10.1016/j.jmb.2007.08.015;
Huang W.C., Westlake A.C., Marechal J.D., Joyce M.G., Moody P.C.,
Roberts G.C.;
"Filling a hole in cytochrome P450 BM3 improves substrate binding and
catalytic efficiency.";
J. Mol. Biol. 373:633-651(2007).
[22] {ECO:0000244|PDB:3BEN}
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-470 IN COMPLEX WITH HEME
AND SUBSTRATE INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, AND ENZYME
REGULATION.
PubMed=18298086; DOI=10.1021/bi7023964;
Haines D.C., Chen B., Tomchick D.R., Bondlela M., Hegde A.,
Machius M., Peterson J.A.;
"Crystal structure of inhibitor-bound P450BM-3 reveals open
conformation of substrate access channel.";
Biochemistry 47:3662-3670(2008).
[23] {ECO:0000244|PDB:3CBD}
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-456 OF
MUTANT ALA-79/TYR-139/ILE-176/ILE-179/VAL-185/GLN-237/GLY-253/SER-
256/VAL-291/THR-296/VAL-354 IN COMPLEX WITH HEME AND
N-PALMITOYLGLYCINE, FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
PubMed=18619466; DOI=10.1016/j.jmb.2008.06.060;
Fasan R., Meharenna Y.T., Snow C.D., Poulos T.L., Arnold F.H.;
"Evolutionary history of a specialized p450 propane monooxygenase.";
J. Mol. Biol. 383:1069-1080(2008).
[24] {ECO:0000244|PDB:3EKB, ECO:0000244|PDB:3EKD, ECO:0000244|PDB:3EKF}
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-471 OF MUTANTS
CYS/MET/GLN-265 IN COMPLEXES WITH HEME AND PALMITOLEIC ACID, FUNCTION,
CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
SPECTROSCOPIC STUDIES, REDOX POTENTIOMETRY OF HEME, AND MUTAGENESIS OF
ALA-265.
PubMed=18721129; DOI=10.1042/BJ20081133;
Girvan H.M., Toogood H.S., Littleford R.E., Seward H.E., Smith W.E.,
Ekanem I.S., Leys D., Cheesman M.R., Munro A.W.;
"Novel haem co-ordination variants of flavocytochrome P450BM3.";
Biochem. J. 417:65-76(2009).
[25] {ECO:0000244|PDB:3HF2}
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-482 OF MUTANT PRO-402 IN
COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, REDOX POTENTIOMETRY OF HEME,
BIOTECHNOLOGY, AND MUTAGENESIS OF ILE-402.
PubMed=19492389; DOI=10.1002/cbic.200900279;
Whitehouse C.J., Bell S.G., Yang W., Yorke J.A., Blanford C.F.,
Strong A.J., Morse E.J., Bartlam M., Rao Z., Wong L.L.;
"A highly active single-mutation variant of P450BM3 (CYP102A1).";
ChemBioChem 10:1654-1656(2009).
[26] {ECO:0000244|PDB:3KX3, ECO:0000244|PDB:3KX4, ECO:0000244|PDB:3KX5}
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 2-471 OF MUTANTS GLU-87;
GLU-262 AND GLU-402 IN COMPLEXES WITH HEME AND N-PALMITOYLGLYCINE,
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
REDOX POTENTIOMETRY OF HEME, AND MUTAGENESIS OF LEU-87; PHE-262 AND
ILE-402.
PubMed=20180779; DOI=10.1042/BJ20091603;
Girvan H.M., Levy C.W., Williams P., Fisher K., Cheesman M.R.,
Rigby S.E., Leys D., Munro A.W.;
"Glutamate-haem ester bond formation is disfavoured in flavocytochrome
P450 BM3: characterization of glutamate substitution mutants at the
haem site of P450 BM3.";
Biochem. J. 427:455-466(2010).
[27] {ECO:0000244|PDB:3M4V}
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-482 OF MUTANT PRO-331 IN
COMPLEX WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, REDOX POTENTIOMETRY OF HEME,
BIOTECHNOLOGY, AND MUTAGENESIS OF ALA-331.
PubMed=21110374; DOI=10.1002/cbic.201000421;
Whitehouse C.J., Yang W., Yorke J.A., Rowlatt B.C., Strong A.J.,
Blanford C.F., Bell S.G., Bartlam M., Wong L.L., Rao Z.;
"Structural basis for the properties of two single-site proline
mutants of CYP102A1 (P450BM3).";
ChemBioChem 11:2549-2556(2010).
[28] {ECO:0000244|PDB:3NPL}
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-464 OF MUTANT
ALA-63/CYS-98/CYS-157 IN COMPLEX WITH HEME, AND REACTION MECHANISM.
PubMed=20947800; DOI=10.1073/pnas.1012381107;
Ener M.E., Lee Y.T., Winkler J.R., Gray H.B., Cheruzel L.;
"Photooxidation of cytochrome P450-BM3.";
Proc. Natl. Acad. Sci. U.S.A. 107:18783-18786(2010).
[29] {ECO:0000244|PDB:1ZO4, ECO:0000244|PDB:1ZOA}
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-471 IN COMPLEXES WITH HEME
AND N-PALMITOYLGLYCINE, FUNCTION, CATALYTIC ACTIVITY, ENZYME KINETICS,
AND MUTAGENESIS OF ALA-329.
PubMed=21875028; DOI=10.1021/bi201099j;
Haines D.C., Hegde A., Chen B., Zhao W., Bondlela M., Humphreys J.M.,
Mullin D.A., Tomchick D.R., Machius M., Peterson J.A.;
"A single active-site mutation of P450BM-3 dramatically enhances
substrate binding and rate of product formation.";
Biochemistry 50:8333-8341(2011).
-!- FUNCTION: Functions as a fatty acid monooxygenase (PubMed:3106359,
PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892,
PubMed:14653735, PubMed:16403573, PubMed:18004886,
PubMed:17077084, PubMed:17868686, PubMed:18298086,
PubMed:18619466, PubMed:18721129, PubMed:19492389,
PubMed:20180779, PubMed:21110374, PubMed:21875028). Catalyzes
hydroxylation of fatty acids at omega-1, omega-2 and omega-3
positions (PubMed:1727637, PubMed:21875028). Shows activity toward
medium and long-chain fatty acids, with optimum chain lengths of
12, 14 and 16 carbons (lauric, myristic, and palmitic acids). Able
to metabolize some of these primary metabolites to secondary and
tertiary products (PubMed:1727637). Marginal activity towards
short chain lengths of 8-10 carbons (PubMed:1727637,
PubMed:18619466). Hydroxylates highly branched fatty acids, which
play an essential role in membrane fluidity regulation
(PubMed:16566047). Also displays a NADPH-dependent reductase
activity in the C-terminal domain, which allows electron transfer
from NADPH to the heme iron of the cytochrome P450 N-terminal
domain (PubMed:3106359, PubMed:1727637, PubMed:16566047,
PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573,
PubMed:18004886, PubMed:17077084, PubMed:17868686,
PubMed:18298086, PubMed:18619466, PubMed:18721129,
PubMed:19492389, PubMed:20180779, PubMed:21110374,
PubMed:21875028). Involved in inactivation of quorum sensing
signals of other competing bacteria by oxidazing efficiently acyl
homoserine lactones (AHLs), molecules involved in quorum sensing
signaling pathways, and their lactonolysis products acyl
homoserines (AHs) (PubMed:18020460). {ECO:0000269|PubMed:11695892,
ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:16403573,
ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:17077084,
ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:17868686,
ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18020460,
ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466,
ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389,
ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374,
ECO:0000269|PubMed:21875028, ECO:0000269|PubMed:3106359,
ECO:0000269|PubMed:7578081}.
-!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
reduced hemoprotein. {ECO:0000269|PubMed:11695889,
ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:14653735,
ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:16566047,
ECO:0000269|PubMed:17077084, ECO:0000269|PubMed:1727637,
ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886,
ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:18298086,
ECO:0000269|PubMed:18619466, ECO:0000269|PubMed:18721129,
ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779,
ECO:0000269|PubMed:21110374, ECO:0000269|PubMed:21875028,
ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081}.
-!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
{ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892,
ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:16403573,
ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:17077084,
ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:17868686,
ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18020460,
ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466,
ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389,
ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374,
ECO:0000269|PubMed:21875028, ECO:0000269|PubMed:3106359,
ECO:0000269|PubMed:7578081}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:7578081};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:10051560};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:16403573,
ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389,
ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374};
-!- ENZYME REGULATION: Inhibited by N-(12-imidazolyl-dodecanoyl)-L-
leucine. {ECO:0000269|PubMed:18298086}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=250 uM for lauric acid at pH 7.4 at room temperature
{ECO:0000269|PubMed:18020460};
KM=34 uM for N-beta-oxolauroyl-DL-homoserine lactone
{ECO:0000269|PubMed:18020460};
KM=210 uM for N-beta-oxolauroyl-DL-homoserine
{ECO:0000269|PubMed:18020460};
KM=140 uM for N-lauroyl-DL-homoserine
{ECO:0000269|PubMed:18020460};
KM=322 uM for lauric acid at pH 7.5 and 15 degrees Celsius
{ECO:0000269|PubMed:16403573};
KM=265 uM for lauric acid {ECO:0000269|PubMed:17868686};
KM=16 mM for indole {ECO:0000269|PubMed:17868686};
KM=87.4 uM for laurate/dodecanoate at pH 7.0 and 25 degrees
Celsius {ECO:0000269|PubMed:18721129};
KM=230 uM for lauric acid at pH 7.4
{ECO:0000269|PubMed:19492389};
KM=87.4 uM for laurate/dodecanoate at 25 degrees Celsius
{ECO:0000269|PubMed:20180779};
KM=5.1 uM for arachidonate at 25 degrees Celsius
{ECO:0000269|PubMed:20180779};
KM=42.4 uM for palmitic acid at pH 7.4 and 30 degrees Celsius
{ECO:0000269|PubMed:21110374};
Note=kcat is 84.1 s(-1) for lauric acid (PubMed:16403573). kcat
is 1480 min(-1) for palmitic acid. kcat is 1880 min(-1) for N-
palmitoylglycine. kcat is 1690 min(-1) for N-palmitoyl-L-
methionine. kcat is 610 min(-1) for N-palmitoyl-L-glutamine.
kcat is 485 min(-1) for N-palmitoyl-L-glutamic acid. kcat is
1160 min(-1) for N-palmitoyl-L-leucine (PubMed:18004886). kcat
is 28 s(-1) for lauric acid (PubMed:17868686). kcat is 2770
min(-1) for laurate/dodecanoate (PubMed:18721129). kcat is 77
for lauric acid (PubMed:19492389). kcat is 2770 min(-1) for
laurate/dodecanoate (PubMed:20180779). kcat is 16400 min(-1) for
arachidonate (PubMed:20180779). kcat is 91.4 for palmitic acid
(PubMed:21110374). {ECO:0000269|PubMed:16403573,
ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886,
ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389,
ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374};
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-7701704, EBI-7701704;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- INDUCTION: By pentobarbital (PubMed:1544926, PubMed:3106359).
Expression is negatively regulated by repressor bm3R1 at the
transcriptional level (PubMed:1544926).
{ECO:0000269|PubMed:1544926, ECO:0000269|PubMed:3106359}.
-!- BIOTECHNOLOGY: This protein is a target of protein engineering.
Its selectivity-directing and activity-enhancing mutations have
been extensively studied and the designed mutations allow this
enzyme to act on non-native substrates and/or in order to enhance
production of synthetically desirable end-products.
{ECO:0000269|PubMed:18619466, ECO:0000269|PubMed:19492389,
ECO:0000269|PubMed:21110374, ECO:0000305}.
-!- SIMILARITY: In the N-terminal section; belongs to the cytochrome
P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J04832; AAA87602.1; -; Genomic_DNA.
EMBL; CP009920; AJI21949.1; -; Genomic_DNA.
EMBL; S87512; AAK19020.1; -; Genomic_DNA.
PIR; A34286; A34286.
RefSeq; WP_034650526.1; NZ_JJMH01000056.1.
PDB; 1BU7; X-ray; 1.65 A; A/B=2-456.
PDB; 1BVY; X-ray; 2.03 A; A/B=2-459, F=460-650.
PDB; 1FAG; X-ray; 2.70 A; A/B/C/D=2-472.
PDB; 1FAH; X-ray; 2.30 A; A/B=2-472.
PDB; 1JME; X-ray; 2.00 A; A/B=2-456.
PDB; 1JPZ; X-ray; 1.65 A; A/B=2-471.
PDB; 1P0V; X-ray; 2.05 A; A/B=2-456.
PDB; 1P0W; X-ray; 2.00 A; A/B=2-456.
PDB; 1P0X; X-ray; 2.00 A; A/B=2-456.
PDB; 1SMI; X-ray; 2.00 A; A/B=2-472.
PDB; 1SMJ; X-ray; 2.75 A; A/B/C/D=2-472.
PDB; 1YQO; X-ray; 1.90 A; A/B=2-456.
PDB; 1YQP; X-ray; 1.80 A; A/B=2-456.
PDB; 1ZO4; X-ray; 1.46 A; A/B=2-471.
PDB; 1ZO9; X-ray; 1.70 A; A/B=2-471.
PDB; 1ZOA; X-ray; 1.74 A; A/B=2-471.
PDB; 2BMH; X-ray; 2.00 A; A/B=2-456.
PDB; 2HPD; X-ray; 2.00 A; A/B=2-472.
PDB; 2IJ2; X-ray; 1.20 A; A/B=2-471.
PDB; 2IJ3; X-ray; 1.90 A; A/B=2-471.
PDB; 2IJ4; X-ray; 2.40 A; A/B=2-471.
PDB; 2J1M; X-ray; 1.70 A; A/B=2-456.
PDB; 2J4S; X-ray; 2.10 A; A/B=2-456.
PDB; 2NNB; X-ray; 1.90 A; A/B=2-472.
PDB; 2UWH; X-ray; 2.80 A; A/B/C/D/E/F=2-459.
PDB; 2X7Y; X-ray; 2.10 A; A/B=2-456.
PDB; 2X80; X-ray; 2.30 A; A/B=2-456.
PDB; 3BEN; X-ray; 1.65 A; A/B=1-470.
PDB; 3CBD; X-ray; 2.65 A; A/B=2-456.
PDB; 3DGI; X-ray; 1.95 A; A/B=2-456.
PDB; 3EKB; X-ray; 2.30 A; A/B=2-471.
PDB; 3EKD; X-ray; 2.50 A; A/B=2-471.
PDB; 3EKF; X-ray; 2.10 A; A/B=2-471.
PDB; 3HF2; X-ray; 2.20 A; A/B=1-482.
PDB; 3KX3; X-ray; 1.80 A; A/B=2-471.
PDB; 3KX4; X-ray; 1.95 A; A/B=2-471.
PDB; 3KX5; X-ray; 1.69 A; A/B=2-471.
PDB; 3M4V; X-ray; 1.90 A; A/B=1-482.
PDB; 3NPL; X-ray; 2.40 A; A/B=1-464.
PDB; 3PSX; X-ray; 1.90 A; A/B=1-482.
PDB; 3WSP; X-ray; 1.80 A; A/B=1-456.
PDB; 4DQK; X-ray; 2.40 A; A/B=659-1049.
PDB; 4DQL; X-ray; 2.15 A; A/B=657-1049.
PDB; 4DTW; X-ray; 1.80 A; A/B=2-464.
PDB; 4DTY; X-ray; 1.45 A; A/B=2-464.
PDB; 4DTZ; X-ray; 1.55 A; A/B=2-464.
PDB; 4DU2; X-ray; 1.90 A; A/B=1-464.
PDB; 4DUA; X-ray; 2.00 A; A/B=2-464.
PDB; 4DUB; X-ray; 1.70 A; A/B=1-464.
PDB; 4DUC; X-ray; 1.92 A; A/B=1-464.
PDB; 4DUD; X-ray; 1.85 A; A/B=2-464.
PDB; 4DUE; X-ray; 1.70 A; A/B=2-464.
PDB; 4DUF; X-ray; 1.80 A; A/B/C/D=2-464.
PDB; 4H23; X-ray; 3.30 A; A/B=1-464.
PDB; 4H24; X-ray; 2.50 A; A/B/C/D=1-464.
PDB; 4HGF; X-ray; 1.70 A; A/B=2-456.
PDB; 4HGG; X-ray; 1.70 A; A/B=2-456.
PDB; 4HGH; X-ray; 1.40 A; A/B=2-456.
PDB; 4HGI; X-ray; 1.50 A; A/B=2-456.
PDB; 4HGJ; X-ray; 1.90 A; A/B=2-456.
PDB; 4KEW; X-ray; 1.89 A; A/B=2-456.
PDB; 4KEY; X-ray; 2.05 A; A/B=2-456.
PDB; 4KF0; X-ray; 1.45 A; A/B=2-458.
PDB; 4KF2; X-ray; 1.82 A; A/B=2-458.
PDB; 4KPA; X-ray; 2.00 A; A=1-471.
PDB; 4KPB; X-ray; 2.10 A; A/B=1-471.
PDB; 4O4P; X-ray; 1.83 A; A/B=2-456.
PDB; 4RSN; X-ray; 2.70 A; A/B=1-456.
PDB; 4WG2; X-ray; 2.66 A; A/B/C=2-464.
PDB; 4ZF6; X-ray; 2.77 A; A=1-461.
PDB; 4ZF8; X-ray; 2.77 A; A=1-461.
PDB; 4ZFA; X-ray; 2.77 A; A=1-461.
PDB; 4ZFB; X-ray; 2.84 A; A=1-461.
PDB; 5B2U; X-ray; 1.90 A; A/B=1-456.
PDB; 5B2V; X-ray; 2.30 A; A/B=1-456.
PDB; 5B2W; X-ray; 1.65 A; A/B=1-456.
PDB; 5B2X; X-ray; 1.90 A; A/B=1-456.
PDB; 5B2Y; X-ray; 2.01 A; A/B=1-456.
PDB; 5DYP; X-ray; 2.40 A; A/C=2-471.
PDB; 5DYZ; X-ray; 1.97 A; A/C=2-471.
PDB; 5E78; X-ray; 2.00 A; A/B=2-456.
PDB; 5E7Y; X-ray; 2.00 A; A/B=2-472.
PDB; 5E9Z; X-ray; 2.23 A; A/B/C/D=1-468.
PDB; 5JQ2; X-ray; 2.00 A; A/B=2-464.
PDB; 5JQU; X-ray; 2.16 A; A/B/C/D/E/F/G/H=2-464.
PDB; 5JQV; X-ray; 2.34 A; A/B/C/D/E/F/G/H=2-464.
PDB; 5JTD; X-ray; 1.50 A; A/B=2-464.
PDB; 5UCW; X-ray; 1.70 A; A/B=1-464.
PDB; 5XA3; X-ray; 2.20 A; A/B/C/D=1-456.
PDB; 5XHJ; X-ray; 2.00 A; A/B=1-456.
PDBsum; 1BU7; -.
PDBsum; 1BVY; -.
PDBsum; 1FAG; -.
PDBsum; 1FAH; -.
PDBsum; 1JME; -.
PDBsum; 1JPZ; -.
PDBsum; 1P0V; -.
PDBsum; 1P0W; -.
PDBsum; 1P0X; -.
PDBsum; 1SMI; -.
PDBsum; 1SMJ; -.
PDBsum; 1YQO; -.
PDBsum; 1YQP; -.
PDBsum; 1ZO4; -.
PDBsum; 1ZO9; -.
PDBsum; 1ZOA; -.
PDBsum; 2BMH; -.
PDBsum; 2HPD; -.
PDBsum; 2IJ2; -.
PDBsum; 2IJ3; -.
PDBsum; 2IJ4; -.
PDBsum; 2J1M; -.
PDBsum; 2J4S; -.
PDBsum; 2NNB; -.
PDBsum; 2UWH; -.
PDBsum; 2X7Y; -.
PDBsum; 2X80; -.
PDBsum; 3BEN; -.
PDBsum; 3CBD; -.
PDBsum; 3DGI; -.
PDBsum; 3EKB; -.
PDBsum; 3EKD; -.
PDBsum; 3EKF; -.
PDBsum; 3HF2; -.
PDBsum; 3KX3; -.
PDBsum; 3KX4; -.
PDBsum; 3KX5; -.
PDBsum; 3M4V; -.
PDBsum; 3NPL; -.
PDBsum; 3PSX; -.
PDBsum; 3WSP; -.
PDBsum; 4DQK; -.
PDBsum; 4DQL; -.
PDBsum; 4DTW; -.
PDBsum; 4DTY; -.
PDBsum; 4DTZ; -.
PDBsum; 4DU2; -.
PDBsum; 4DUA; -.
PDBsum; 4DUB; -.
PDBsum; 4DUC; -.
PDBsum; 4DUD; -.
PDBsum; 4DUE; -.
PDBsum; 4DUF; -.
PDBsum; 4H23; -.
PDBsum; 4H24; -.
PDBsum; 4HGF; -.
PDBsum; 4HGG; -.
PDBsum; 4HGH; -.
PDBsum; 4HGI; -.
PDBsum; 4HGJ; -.
PDBsum; 4KEW; -.
PDBsum; 4KEY; -.
PDBsum; 4KF0; -.
PDBsum; 4KF2; -.
PDBsum; 4KPA; -.
PDBsum; 4KPB; -.
PDBsum; 4O4P; -.
PDBsum; 4RSN; -.
PDBsum; 4WG2; -.
PDBsum; 4ZF6; -.
PDBsum; 4ZF8; -.
PDBsum; 4ZFA; -.
PDBsum; 4ZFB; -.
PDBsum; 5B2U; -.
PDBsum; 5B2V; -.
PDBsum; 5B2W; -.
PDBsum; 5B2X; -.
PDBsum; 5B2Y; -.
PDBsum; 5DYP; -.
PDBsum; 5DYZ; -.
PDBsum; 5E78; -.
PDBsum; 5E7Y; -.
PDBsum; 5E9Z; -.
PDBsum; 5JQ2; -.
PDBsum; 5JQU; -.
PDBsum; 5JQV; -.
PDBsum; 5JTD; -.
PDBsum; 5UCW; -.
PDBsum; 5XA3; -.
PDBsum; 5XHJ; -.
ProteinModelPortal; P14779; -.
SMR; P14779; -.
MINT; P14779; -.
BindingDB; P14779; -.
DrugBank; DB08086; N-[12-(1H-imidazol-1-yl)dodecanoyl]-L-leucine.
DrugBank; DB03440; N-Hexadecanoylglycine.
DrugBank; DB04257; Palmitoleic Acid.
EnsemblBacteria; AJI21949; AJI21949; BG04_163.
GeneID; 29911283; -.
KEGG; bmeg:BG04_163; -.
eggNOG; ENOG4107EER; Bacteria.
eggNOG; COG0369; LUCA.
KO; K14338; -.
BioCyc; MetaCyc:MONOMER-17698; -.
BRENDA; 1.14.14.1; 656.
BRENDA; 1.6.2.4; 656.
EvolutionaryTrace; P14779; -.
Proteomes; UP000031829; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070330; F:aromatase activity; IDA:UniProtKB.
GO; GO:0010181; F:FMN binding; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:UniProtKB.
GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
Gene3D; 1.20.990.10; -; 1.
Gene3D; 3.40.50.360; -; 1.
InterPro; IPR023206; Bifunctional_P450_P450_red.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR036396; Cyt_P450_sf.
InterPro; IPR003097; FAD-binding_1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
Pfam; PF00067; p450; 1.
PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SUPFAM; SSF48264; SSF48264; 1.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Electron transport; FAD;
Flavoprotein; FMN; Heme; Iron; Metal-binding; Monooxygenase;
Multifunctional enzyme; NADP; Oxidoreductase; Transport.
CHAIN 1 1049 Bifunctional cytochrome P450/NADPH--P450
reductase.
/FTId=PRO_0000052205.
DOMAIN 483 622 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 660 892 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 489 494 FMN. {ECO:0000244|PDB:1BVY,
ECO:0000269|PubMed:10051560}.
NP_BIND 536 539 FMN. {ECO:0000244|PDB:1BVY,
ECO:0000269|PubMed:10051560}.
NP_BIND 570 572 FMN. {ECO:0000244|PDB:1BVY,
ECO:0000269|PubMed:10051560}.
NP_BIND 578 580 FMN. {ECO:0000244|PDB:1BVY,
ECO:0000269|PubMed:10051560}.
REGION 2 472 Cytochrome P450.
REGION 473 1049 NADPH--P450 reductase.
METAL 401 401 Iron (heme axial ligand).
{ECO:0000244|PDB:1BU7,
ECO:0000244|PDB:1BVY,
ECO:0000244|PDB:1FAG,
ECO:0000244|PDB:1FAH,
ECO:0000244|PDB:1JME,
ECO:0000244|PDB:1JPZ,
ECO:0000244|PDB:1P0V,
ECO:0000244|PDB:1P0W,
ECO:0000244|PDB:1P0X,
ECO:0000244|PDB:1SMI,
ECO:0000244|PDB:1SMJ,
ECO:0000244|PDB:1YQO,
ECO:0000244|PDB:1YQP,
ECO:0000244|PDB:1ZO4,
ECO:0000244|PDB:1ZO9,
ECO:0000244|PDB:1ZOA,
ECO:0000244|PDB:2BMH,
ECO:0000244|PDB:2HPD,
ECO:0000244|PDB:2IJ2,
ECO:0000244|PDB:2IJ3,
ECO:0000244|PDB:2IJ4,
ECO:0000244|PDB:2J1M,
ECO:0000244|PDB:2J4S,
ECO:0000244|PDB:2UWH,
ECO:0000244|PDB:3BEN,
ECO:0000244|PDB:3CBD,
ECO:0000244|PDB:3EKB,
ECO:0000244|PDB:3EKD,
ECO:0000244|PDB:3EKF,
ECO:0000244|PDB:3HF2,
ECO:0000244|PDB:3KX3,
ECO:0000244|PDB:3KX4,
ECO:0000244|PDB:3KX5,
ECO:0000244|PDB:3M4V,
ECO:0000244|PDB:3NPL,
ECO:0000269|PubMed:10051560,
ECO:0000269|PubMed:11695889,
ECO:0000269|PubMed:11695892,
ECO:0000269|PubMed:14653735,
ECO:0000269|PubMed:15020590,
ECO:0000269|PubMed:15299332,
ECO:0000269|PubMed:16403573,
ECO:0000269|PubMed:17077084,
ECO:0000269|PubMed:17429965,
ECO:0000269|PubMed:17868686,
ECO:0000269|PubMed:18004886,
ECO:0000269|PubMed:18298086,
ECO:0000269|PubMed:18619466,
ECO:0000269|PubMed:18721129,
ECO:0000269|PubMed:19492389,
ECO:0000269|PubMed:20180779,
ECO:0000269|PubMed:20947800,
ECO:0000269|PubMed:21110374,
ECO:0000269|PubMed:21875028,
ECO:0000269|PubMed:7578081,
ECO:0000269|PubMed:8342039,
ECO:0000269|PubMed:9033595}.
BINDING 52 52 Fatty acid. {ECO:0000244|PDB:1SMJ,
ECO:0000269|PubMed:15020590}.
SITE 269 269 Important for catalytic activity.
{ECO:0000305|PubMed:16403573,
ECO:0000305|PubMed:7578081}.
MUTAGEN 48 48 R->Q,S: 2-3-fold decrease in binding
affinity for N-myristoyl-L-methionine as
substrate. {ECO:0000269|PubMed:18004886}.
MUTAGEN 75 75 A->G: Higher activity in the
hydroxylation of highly branched fatty
acids; when associated with V-88 and Q-
189. {ECO:0000269|PubMed:16566047}.
MUTAGEN 83 83 A->F: 800-fold binding affinity for
laurate as substrate. High coupling of
NADPH consumption to laurate formation.
Very much more effective in indole
hydroxylation. Favors omega-2
hydroxylation. Significantly higher rates
of NADPH consumption in the absence of
substrate. No temperature-dependent
shifts to low-spin in complex with
palmitate. {ECO:0000269|PubMed:17868686}.
MUTAGEN 83 83 A->I: No effect in binding affinity for
laurate as substrate. High coupling of
NADPH consumption to laurate formation.
No indole hydroxylation. Favors omega-2
hydroxylation. Similarly to wild-type,
shows significant shifts to low-spin in
complex with palmitate as the temperature
decreases. {ECO:0000269|PubMed:17868686}.
MUTAGEN 83 83 A->W: 800-fold binding affinity for
laurate as substrate. Low coupling of
NADPH consumption to laurate formation.
Very much more effective in indole
hydroxylation. Favors omega-1
hydroxylation. Significantly higher rates
of NADPH consumption in the absence of
substrate. No temperature-dependent
shifts to low-spin in complex with
palmitate. {ECO:0000269|PubMed:17868686}.
MUTAGEN 87 87 L->E: Ineffective covalent modification
of the heme macrocycle. Extensive
formation of Fe(II)CO complex in the
substrate-free form. Has more positive
potential in both substrate-free and
arachidonate-bound forms and some high-
spin content in the ferric substrate-free
form of the enzyme.
{ECO:0000269|PubMed:20180779}.
MUTAGEN 88 88 F->V: Higher activity in the
hydroxylation of highly branched fatty
acids; when associated with G-75 and Q-
189. {ECO:0000269|PubMed:16566047}.
MUTAGEN 189 189 L->Q: Higher activity in the
hydroxylation of highly branched fatty
acids; when associated with G-75 and V-
88. {ECO:0000269|PubMed:16566047}.
MUTAGEN 262 262 F->E: Ineffective covalent modification
of the heme macrocycle. Substantially
slower FMN to heme electron transfer for
the arachidonate-bound enzyme. Product
distribution biased towards omega-3.
{ECO:0000269|PubMed:20180779}.
MUTAGEN 265 265 A->C: No effective fatty acid oxidation.
No effect on electron transport from
NADPH to FMN. Substantially lower high-
spin conversion with arachidonate and
palmitoleate, and negligible change is
observed with palmitate, myristate and
laurate/dodecanoate. 20% of omega-1,
omega-2 and omega-3 laurate/dodecanoate
hydroxylation products.
{ECO:0000269|PubMed:18721129}.
MUTAGEN 265 265 A->H,K: No significant stimulation of
NADPH oxidation induced by addition of
fatty acids and no hydroxylated products,
but cytochrome c reductase activity
levels are identical to wild-type enzyme.
More negative reduction potential with
dithionite. Unable to form Fe(2+)CO
complexes on reduction with dithionite
and bubbling with carbon monoxide.
{ECO:0000269|PubMed:17077084}.
MUTAGEN 265 265 A->M: No effective fatty acid oxidation.
No effect on electron transport from
NADPH to FMN. Slightly lower high-spin
conversion with arachidonate,
palmitoleate, palmitate, myristate and
laurate/dodecanoate. 5% of omega-1,
omega-2 and omega-3 laurate/dodecanoate
hydroxylation products.
{ECO:0000269|PubMed:18721129}.
MUTAGEN 265 265 A->Q: No effective fatty acid oxidation.
No effect on electron transport from
NADPH to FMN. Nearly wild-type level of
high-spin conversion with
laurate/dodecanoate, palmitoleate and
arachidonate. 5% of omega-1, omega-2 and
omega-3 laurate/dodecanoate hydroxylation
products. {ECO:0000269|PubMed:18721129}.
MUTAGEN 269 269 T->A: Contrary to wild-type, significant
decrease in the formation of the high-
spin complex via substrate binding, and
decreased substrate-induced reduction
potential shift with saturating
concentrations of arachidonate; when
associated with H-394. Considerably lower
proportion of high-spin protein and
decreased substrate-induced heme
reduction-potential shift on addition of
saturating concentrations of
arachidonate. Leads to destabilisation of
the oxy-ferrous complex. Exhibits slower
rates of O(2) and NADPH consumption using
sodium laurate as the substrate. Greater
production of water and peroxide compared
to wild-type indicating uncoupled
electron transfer from sodium laurate
hydroxylation. Only 16% yield of product
after 5 min of reaction relative to the
amount of NADPH used compared to 100% of
wild-type. {ECO:0000269|PubMed:16403573,
ECO:0000269|PubMed:7578081}.
MUTAGEN 269 269 T->N: High substrate-free turnover rate
constant. Negligible substrate-induced
spin-state and substrate-induced heme
reduction-potential shifts on addition of
saturating concentrations of
arachidonate. Induces a positive shift in
the substrate-free heme reduction
potential. 10-fold greater rate constants
for the first electron transfer in the
absence of substrate; when associated
with H-394. Turnover rate constants
diminished. Significantly smaller degrees
of coupling to product. Negligible
amounts of high-spin protein on addition
of saturating concentration of
arachidonate. Negligible substrate-
induced spin-state and substrate-induced
heme reduction-potential shifts on
addition of saturating concentrations of
arachidonate. Induces a 60 mV positive
shift in the substrate-free heme
reduction potential. The apparent rate
constant for heme reduction is smaller
than the overall turnover rate constant.
Leads to destabilisation of the oxy-
ferrous complex.
{ECO:0000269|PubMed:16403573}.
MUTAGEN 329 329 A->V: Substrate binding affinity
increases 5-10 fold and the turnover
number increases 2-8-fold for palmitate
as substrate compared to the wild-type.
Has a very different product distribution
favoring greatly oxidation at the omega-1
position and shows almost no oxidation at
the omega-3 position.
{ECO:0000269|PubMed:21875028}.
MUTAGEN 331 331 A->P: Enhanced activity with small non-
natural substrates with altered product
profiles compared to wild-type.
{ECO:0000269|PubMed:21110374}.
MUTAGEN 394 394 F->H: High substrate-free turnover rate
constant. Negligible substrate-induced
spin-state and substrate-induced heme
reduction-potential shifts on addition of
saturating concentrations of
arachidonate. Induces a positive shift in
the substrate-free heme reduction
potential. 10-fold greater rate constants
for the first electron transfer in the
absence of substrate; when associated
with N-269. Significant decrease in the
formation of the high-spin complex via
substrate binding, and decreased
substrate-induced reduction potential
shift with saturating concentrations of
arachidonate; when associated with A-269.
No change in product profile using
myristate as substrate, but slightly
higher amount of unreacted myristate
indicating lower overall catalytic
activity relative to wild-type.
{ECO:0000269|PubMed:11695889,
ECO:0000269|PubMed:16403573}.
MUTAGEN 394 394 F->W: Large decrease in the heme
reduction potential in the presence and
absence of substrate arachidonate. 10%
reduction in efficiency to couple NADPH
consumption to substrate monooxygenation.
Half of the turn over rate and four times
faster decay of the oxy-ferrous complex
to the ferric form than that of wild-
type. {ECO:0000269|PubMed:14653735}.
MUTAGEN 402 402 I->E: Ineffective covalent modification
of the heme macrocycle. 2-fold apparent
limiting rate of flavin to heme electron
transfer for arachidonate-bound enzyme.
Substrate-free enzyme is converted
rapidly and completely into its Fe(II)CO
complex and has much more positive
potential. 8-fold decrease in overall
catalytic rate with arachidonic acid.
More efficient NADPH oxidase in absence
of fatty acids. Product distribution
biased towards omega-1.
{ECO:0000269|PubMed:20180779}.
MUTAGEN 402 402 I->P: 10-fold increase in binding
affinity for lauric acid. Catalytic
activity rates acclerate across a range
of hydrophobic non-natural substrates,
including (+)-alpha-pinene, fluorene, 3-
methylpentane and propylbenzene, while
product distributions of them are broadly
similar to the wild-type enzyme exept for
(+)-alpha-pinene which is not metabolized
by wild-type.
{ECO:0000269|PubMed:19492389}.
HELIX 13 15 {ECO:0000244|PDB:2IJ2}.
HELIX 18 21 {ECO:0000244|PDB:2IJ2}.
HELIX 26 37 {ECO:0000244|PDB:2IJ2}.
STRAND 39 45 {ECO:0000244|PDB:2IJ2}.
STRAND 48 53 {ECO:0000244|PDB:2IJ2}.
HELIX 56 62 {ECO:0000244|PDB:2IJ2}.
TURN 65 67 {ECO:0000244|PDB:2IJ2}.
STRAND 68 70 {ECO:0000244|PDB:2IJ2}.
HELIX 74 83 {ECO:0000244|PDB:2IJ2}.
HELIX 87 89 {ECO:0000244|PDB:2IJ2}.
STRAND 92 94 {ECO:0000244|PDB:5JQU}.
HELIX 95 104 {ECO:0000244|PDB:2IJ2}.
HELIX 105 108 {ECO:0000244|PDB:2IJ2}.
TURN 110 112 {ECO:0000244|PDB:2IJ2}.
HELIX 113 132 {ECO:0000244|PDB:2IJ2}.
HELIX 142 159 {ECO:0000244|PDB:2IJ2}.
HELIX 165 167 {ECO:0000244|PDB:2IJ2}.
STRAND 169 171 {ECO:0000244|PDB:5JQV}.
HELIX 173 187 {ECO:0000244|PDB:2IJ2}.
HELIX 188 190 {ECO:0000244|PDB:4HGH}.
STRAND 192 194 {ECO:0000244|PDB:4HGJ}.
HELIX 197 199 {ECO:0000244|PDB:2IJ2}.
HELIX 200 227 {ECO:0000244|PDB:2IJ2}.
HELIX 234 240 {ECO:0000244|PDB:2IJ2}.
TURN 244 246 {ECO:0000244|PDB:2IJ2}.
HELIX 252 283 {ECO:0000244|PDB:2IJ2}.
HELIX 285 298 {ECO:0000244|PDB:2IJ2}.
STRAND 301 303 {ECO:0000244|PDB:2IJ2}.
HELIX 306 310 {ECO:0000244|PDB:2IJ2}.
HELIX 313 325 {ECO:0000244|PDB:2IJ2}.
STRAND 331 338 {ECO:0000244|PDB:2IJ2}.
STRAND 340 342 {ECO:0000244|PDB:2IJ2}.
TURN 343 345 {ECO:0000244|PDB:2IJ2}.
STRAND 346 348 {ECO:0000244|PDB:2IJ2}.
STRAND 353 357 {ECO:0000244|PDB:2IJ2}.
HELIX 358 361 {ECO:0000244|PDB:2IJ2}.
HELIX 365 368 {ECO:0000244|PDB:2IJ2}.
TURN 370 373 {ECO:0000244|PDB:4HGH}.
HELIX 377 380 {ECO:0000244|PDB:2IJ2}.
HELIX 383 385 {ECO:0000244|PDB:2IJ2}.
STRAND 388 390 {ECO:0000244|PDB:4ZFB}.
HELIX 397 399 {ECO:0000244|PDB:2IJ2}.
HELIX 404 421 {ECO:0000244|PDB:2IJ2}.
STRAND 422 425 {ECO:0000244|PDB:2IJ2}.
STRAND 434 442 {ECO:0000244|PDB:2IJ2}.
STRAND 446 451 {ECO:0000244|PDB:2IJ2}.
HELIX 462 464 {ECO:0000244|PDB:4WG2}.
STRAND 483 488 {ECO:0000244|PDB:1BVY}.
STRAND 490 492 {ECO:0000244|PDB:1BVY}.
HELIX 493 506 {ECO:0000244|PDB:1BVY}.
TURN 507 509 {ECO:0000244|PDB:1BVY}.
STRAND 513 516 {ECO:0000244|PDB:1BVY}.
HELIX 517 519 {ECO:0000244|PDB:1BVY}.
STRAND 526 534 {ECO:0000244|PDB:1BVY}.
TURN 543 545 {ECO:0000244|PDB:1BVY}.
HELIX 546 553 {ECO:0000244|PDB:1BVY}.
STRAND 565 571 {ECO:0000244|PDB:1BVY}.
HELIX 576 578 {ECO:0000244|PDB:1BVY}.
HELIX 581 591 {ECO:0000244|PDB:1BVY}.
TURN 592 594 {ECO:0000244|PDB:1BVY}.
STRAND 599 605 {ECO:0000244|PDB:1BVY}.
HELIX 610 628 {ECO:0000244|PDB:1BVY}.
STRAND 663 672 {ECO:0000244|PDB:4DQL}.
STRAND 682 688 {ECO:0000244|PDB:4DQL}.
STRAND 700 703 {ECO:0000244|PDB:4DQL}.
HELIX 709 719 {ECO:0000244|PDB:4DQL}.
STRAND 726 729 {ECO:0000244|PDB:4DQK}.
STRAND 741 746 {ECO:0000244|PDB:4DQK}.
HELIX 747 750 {ECO:0000244|PDB:4DQL}.
HELIX 751 753 {ECO:0000244|PDB:4DQK}.
STRAND 756 759 {ECO:0000244|PDB:4DQL}.
HELIX 762 770 {ECO:0000244|PDB:4DQL}.
HELIX 775 783 {ECO:0000244|PDB:4DQL}.
HELIX 787 793 {ECO:0000244|PDB:4DQL}.
TURN 794 798 {ECO:0000244|PDB:4DQL}.
HELIX 801 807 {ECO:0000244|PDB:4DQL}.
HELIX 815 820 {ECO:0000244|PDB:4DQL}.
STRAND 828 831 {ECO:0000244|PDB:4DQL}.
TURN 836 838 {ECO:0000244|PDB:4DQL}.
STRAND 842 848 {ECO:0000244|PDB:4DQL}.
STRAND 851 853 {ECO:0000244|PDB:4DQL}.
STRAND 857 862 {ECO:0000244|PDB:4DQL}.
HELIX 864 871 {ECO:0000244|PDB:4DQL}.
STRAND 877 883 {ECO:0000244|PDB:4DQL}.
STRAND 899 902 {ECO:0000244|PDB:4DQL}.
HELIX 905 908 {ECO:0000244|PDB:4DQL}.
HELIX 909 923 {ECO:0000244|PDB:4DQL}.
STRAND 931 938 {ECO:0000244|PDB:4DQL}.
TURN 940 942 {ECO:0000244|PDB:4DQL}.
HELIX 947 955 {ECO:0000244|PDB:4DQL}.
STRAND 960 967 {ECO:0000244|PDB:4DQL}.
HELIX 976 982 {ECO:0000244|PDB:4DQL}.
HELIX 984 992 {ECO:0000244|PDB:4DQL}.
STRAND 996 1002 {ECO:0000244|PDB:4DQL}.
TURN 1003 1005 {ECO:0000244|PDB:4DQL}.
HELIX 1006 1022 {ECO:0000244|PDB:4DQL}.
HELIX 1026 1038 {ECO:0000244|PDB:4DQL}.
STRAND 1042 1047 {ECO:0000244|PDB:4DQL}.
SEQUENCE 1049 AA; 117781 MW; B0BE61F8A2EE33D5 CRC64;
MTIKEMPQPK TFGELKNLPL LNTDKPVQAL MKIADELGEI FKFEAPGRVT RYLSSQRLIK
EACDESRFDK NLSQALKFVR DFAGDGLFTS WTHEKNWKKA HNILLPSFSQ QAMKGYHAMM
VDIAVQLVQK WERLNADEHI EVPEDMTRLT LDTIGLCGFN YRFNSFYRDQ PHPFITSMVR
ALDEAMNKLQ RANPDDPAYD ENKRQFQEDI KVMNDLVDKI IADRKASGEQ SDDLLTHMLN
GKDPETGEPL DDENIRYQII TFLIAGHETT SGLLSFALYF LVKNPHVLQK AAEEAARVLV
DPVPSYKQVK QLKYVGMVLN EALRLWPTAP AFSLYAKEDT VLGGEYPLEK GDELMVLIPQ
LHRDKTIWGD DVEEFRPERF ENPSAIPQHA FKPFGNGQRA CIGQQFALHE ATLVLGMMLK
HFDFEDHTNY ELDIKETLTL KPEGFVVKAK SKKIPLGGIP SPSTEQSAKK VRKKAENAHN
TPLLVLYGSN MGTAEGTARD LADIAMSKGF APQVATLDSH AGNLPREGAV LIVTASYNGH
PPDNAKQFVD WLDQASADEV KGVRYSVFGC GDKNWATTYQ KVPAFIDETL AAKGAENIAD
RGEADASDDF EGTYEEWREH MWSDVAAYFN LDIENSEDNK STLSLQFVDS AADMPLAKMH
GAFSTNVVAS KELQQPGSAR STRHLEIELP KEASYQEGDH LGVIPRNYEG IVNRVTARFG
LDASQQIRLE AEEEKLAHLP LAKTVSVEEL LQYVELQDPV TRTQLRAMAA KTVCPPHKVE
LEALLEKQAY KEQVLAKRLT MLELLEKYPA CEMKFSEFIA LLPSIRPRYY SISSSPRVDE
KQASITVSVV SGEAWSGYGE YKGIASNYLA ELQEGDTITC FISTPQSEFT LPKDPETPLI
MVGPGTGVAP FRGFVQARKQ LKEQGQSLGE AHLYFGCRSP HEDYLYQEEL ENAQSEGIIT
LHTAFSRMPN QPKTYVQHVM EQDGKKLIEL LDQGAHFYIC GDGSQMAPAV EATLMKSYAD
VHQVSEADAR LWLQQLEEKG RYAKDVWAG


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