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Bifunctional cytochrome P450/NADPH--P450 reductase 1 (CYP102A2) (Fatty acid hydroxylase CypD) (Flavocytochrome P450 102A2) [Includes: Cytochrome P450 102A2 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]

 CYPD_BACSU              Reviewed;        1061 AA.
O08394;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
28-FEB-2018, entry version 141.
RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase 1 {ECO:0000305};
AltName: Full=CYP102A2 {ECO:0000303|PubMed:15122913};
AltName: Full=Fatty acid hydroxylase CypD {ECO:0000305};
AltName: Full=Flavocytochrome P450 102A2 {ECO:0000305};
Includes:
RecName: Full=Cytochrome P450 102A2 {ECO:0000305};
EC=1.14.14.1 {ECO:0000269|PubMed:15122913, ECO:0000269|PubMed:15375636};
Includes:
RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000305};
EC=1.6.2.4 {ECO:0000269|PubMed:15122913, ECO:0000269|PubMed:15375636};
Name=cypD {ECO:0000244|EMBL:CAB12544.1};
Synonyms=cyp102A2 {ECO:0000303|PubMed:15122913,
ECO:0000303|PubMed:15375636}, yetO {ECO:0000303|PubMed:15122913},
yfnJ; OrderedLocusNames=BSU07250;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9308178; DOI=10.1099/00221287-143-9-2939;
Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J.,
Duesterhoeft A., Ehrlich S.D.;
"Sequence of the Bacillus subtilis genome region in the vicinity of
the lev operon reveals two new extracytoplasmic function RNA
polymerase sigma factors SigV and SigZ.";
Microbiology 143:2939-2943(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15375636; DOI=10.1007/s00253-004-1719-y;
Budde M., Maurer S.C., Schmid R.D., Urlacher V.B.;
"Cloning, expression and characterisation of CYP102A2, a self-
sufficient P450 monooxygenase from Bacillus subtilis.";
Appl. Microbiol. Biotechnol. 66:180-186(2004).
[4]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=168 / 1A1;
PubMed=15122913; DOI=10.1021/bi035904m;
Gustafsson M.C., Roitel O., Marshall K.R., Noble M.A., Chapman S.K.,
Pessegueiro A., Fulco A.J., Cheesman M.R., von Wachenfeldt C.,
Munro A.W.;
"Expression, purification, and characterization of Bacillus subtilis
cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of
P450 BM3 from Bacillus megaterium.";
Biochemistry 43:5474-5487(2004).
[5]
PROTEIN ENGINEERING, AND MUTAGENESIS OF PRO-15.
STRAIN=168;
PubMed=15857787; DOI=10.1016/j.bioeng.2004.11.003;
Axarli I., Prigipaki A., Labrou N.E.;
"Engineering the substrate specificity of cytochrome P450 CYP102A2 by
directed evolution: production of an efficient enzyme for
bioconversion of fine chemicals.";
Biomol. Eng. 22:81-88(2005).
[6]
FUNCTION.
PubMed=21048857; DOI=10.4061/2010/125429;
Axarli I., Prigipaki A., Labrou N.E.;
"Cytochrome P450 102A2 catalyzes efficient oxidation of sodium dodecyl
sulphate: a molecular tool for remediation.";
Enzyme Res. 2010:125429-125429(2010).
-!- FUNCTION: Functions as a fatty acid monooxygenase. Catalyzes
hydroxylation of a range of long-chain fatty acids, with a
preference for long-chain unsaturated and branched-chain fatty
acids over saturated fatty acids. Hydroxylation of myristic acid
occurs mainly at the omega-2 position. 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:15375636,
PubMed:15122913). Is also able to catalyze efficient oxidation of
sodium dodecyl sulfate (SDS) (PubMed:21048857).
{ECO:0000269|PubMed:15122913, ECO:0000269|PubMed:15375636,
ECO:0000269|PubMed:21048857}.
-!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
{ECO:0000269|PubMed:15122913, ECO:0000269|PubMed:15375636}.
-!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
reduced hemoprotein. {ECO:0000269|PubMed:15122913,
ECO:0000269|PubMed:15375636}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:15122913};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:15122913};
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:15122913};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=38.8 uM for stearic acid {ECO:0000269|PubMed:15122913};
KM=150 uM for phytanic acid {ECO:0000269|PubMed:15122913};
KM=56.8 uM for 15-methylpalmitic acid
{ECO:0000269|PubMed:15122913};
KM=3.6 uM for NADPH {ECO:0000269|PubMed:15122913};
KM=17.9 mM for NADH {ECO:0000269|PubMed:15122913};
KM=6.9 uM for cytochrome c (in the reductase assay)
{ECO:0000269|PubMed:15122913};
KM=153.4 uM for ferricyanide (in the reductase assay)
{ECO:0000269|PubMed:15122913};
KM=17.36 uM for oleic acid {ECO:0000269|PubMed:15375636};
Note=kcat is 430 min(-1) for stearic acid hydroxylation. kcat is
5430 min(-1) for phytanic acid hydroxylation. kcat is 6105 min(-
1) for 15-methylpalmitic acid hydroxylation. kcat is 11400 min(-
1) for the reduction of cytochrome c. kcat is 38150 min(-1) for
the reduction of ferricyanide (PubMed:15122913). kcat is 2244
min(-1) for oleic acid hydroxylation (PubMed:15375636).
{ECO:0000269|PubMed:15122913, ECO:0000269|PubMed:15375636};
pH dependence:
Optimum pH is 7.0. {ECO:0000269|PubMed:15375636};
Temperature dependence:
Optimum temperature is 51 degrees Celsius. However, enzyme
stability is dramatically reduced at this temperature,
incubation for 30 minutes at 31 and 49 degrees Celsius results
in 61% and 17% residual activity, respectively. Incubation at 60
degrees Celsius leads to total inactivation of the enzyme.
{ECO:0000269|PubMed:15375636};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: In the N-terminal section; belongs to the cytochrome
P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D87979; BAA20123.1; -; Genomic_DNA.
EMBL; AL009126; CAB12544.1; -; Genomic_DNA.
PIR; D69799; D69799.
RefSeq; NP_388606.1; NC_000964.3.
RefSeq; WP_003242884.1; NZ_JNCM01000032.1.
ProteinModelPortal; O08394; -.
SMR; O08394; -.
STRING; 224308.Bsubs1_010100004068; -.
PaxDb; O08394; -.
PRIDE; O08394; -.
EnsemblBacteria; CAB12544; CAB12544; BSU07250.
GeneID; 938784; -.
KEGG; bsu:BSU07250; -.
PATRIC; fig|224308.179.peg.786; -.
eggNOG; ENOG4107EER; Bacteria.
eggNOG; COG0369; LUCA.
eggNOG; COG2124; LUCA.
HOGENOM; HOG000093545; -.
InParanoid; O08394; -.
KO; K14338; -.
OMA; CEIRFER; -.
PhylomeDB; O08394; -.
BioCyc; BSUB:BSU07250-MONOMER; -.
SABIO-RK; O08394; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; ISS: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.
GO; GO:0019395; P:fatty acid oxidation; 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;
Complete proteome; Cytoplasm; Electron transport; FAD; Flavoprotein;
FMN; Heme; Iron; Metal-binding; Monooxygenase; Multifunctional enzyme;
NADP; Oxidoreductase; Reference proteome; Transport.
CHAIN 1 1061 Bifunctional cytochrome P450/NADPH--P450
reductase 1.
/FTId=PRO_0000052206.
DOMAIN 493 632 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 671 904 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 499 504 FMN. {ECO:0000250|UniProtKB:P14779}.
NP_BIND 546 549 FMN. {ECO:0000250|UniProtKB:P14779}.
NP_BIND 580 582 FMN. {ECO:0000250|UniProtKB:P14779}.
NP_BIND 588 590 FMN. {ECO:0000250|UniProtKB:P14779}.
REGION 1 475 Cytochrome P450.
{ECO:0000305|PubMed:15122913}.
REGION 476 1061 NADPH--P450 reductase.
{ECO:0000305|PubMed:15122913}.
METAL 403 403 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P14779}.
SITE 271 271 Important for catalytic activity.
{ECO:0000250|UniProtKB:P14779}.
MUTAGEN 15 15 P->S: Exhibits modified substrate
specificity. Shows approximately 6- to 9-
fold increased activity with SDS, lauric
acid and 1,4-naphthoquinone, and enhanced
activity for other substrates such as
ethacrynic acid and epsilon-amino-n-
caproic acid.
{ECO:0000269|PubMed:15857787}.
SEQUENCE 1061 AA; 119468 MW; 7915DACC20578978 CRC64;
MKETSPIPQP KTFGPLGNLP LIDKDKPTLS LIKLAEEQGP IFQIHTPAGT TIVVSGHELV
KEVCDEERFD KSIEGALEKV RAFSGDGLFT SWTHEPNWRK AHNILMPTFS QRAMKDYHEK
MVDIAVQLIQ KWARLNPNEA VDVPGDMTRL TLDTIGLCGF NYRFNSYYRE TPHPFINSMV
RALDEAMHQM QRLDVQDKLM VRTKRQFRYD IQTMFSLVDS IIAERRANGD QDEKDLLARM
LNVEDPETGE KLDDENIRFQ IITFLIAGHE TTSGLLSFAT YFLLKHPDKL KKAYEEVDRV
LTDAAPTYKQ VLELTYIRMI LNESLRLWPT APAFSLYPKE DTVIGGKFPI TTNDRISVLI
PQLHRDRDAW GKDAEEFRPE RFEHQDQVPH HAYKPFGNGQ RACIGMQFAL HEATLVLGMI
LKYFTLIDHE NYELDIKQTL TLKPGDFHIS VQSRHQEAIH ADVQAAEKAA PDEQKEKTEA
KGASVIGLNN RPLLVLYGSD TGTAEGVARE LADTASLHGV RTKTAPLNDR IGKLPKEGAV
VIVTSSYNGK PPSNAGQFVQ WLQEIKPGEL EGVHYAVFGC GDHNWASTYQ YVPRFIDEQL
AEKGATRFSA RGEGDVSGDF EGQLDEWKKS MWADAIKAFG LELNENADKE RSTLSLQFVR
GLGESPLARS YEASHASIAE NRELQSADSD RSTRHIEIAL PPDVEYQEGD HLGVLPKNSQ
TNVSRILHRF GLKGTDQVTL SASGRSAGHL PLGRPVSLHD LLSYSVEVQE AATRAQIREL
ASFTVCPPHR RELEELSAEG VYQEQILKKR ISMLDLLEKY EACDMPFERF LELLRPLKPR
YYSISSSPRV NPRQASITVG VVRGPAWSGR GEYRGVASND LAERQAGDDV VMFIRTPESR
FQLPKDPETP IIMVGPGTGV APFRGFLQAR DVLKREGKTL GEAHLYFGCR NDRDFIYRDE
LERFEKDGIV TVHTAFSRKE GMPKTYVQHL MADQADTLIS ILDRGGRLYV CGDGSKMAPD
VEAALQKAYQ AVHGTGEQEA QNWLRHLQDT GMYAKDVWAG I


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6017 Snell Ave, Ste 357
San Jose, CA 95123




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