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Methyl-branched lipid omega-hydroxylase (EC 1.14.15.14) (Cholest-4-en-3-one C26-monooxygenase) (Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]) (Cholesterol C26-monooxygenase) (Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming]) (Cytochrome P450 124) (Steroid C26-monooxygenase) (EC 1.14.13.221) (Steroid C27-monooxygenase)

 CP124_MYCTU             Reviewed;         428 AA.
P9WPP3; L0TBS5; P0A516; Q50696;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
25-OCT-2017, entry version 29.
RecName: Full=Methyl-branched lipid omega-hydroxylase {ECO:0000303|PubMed:19933331};
EC=1.14.15.14 {ECO:0000269|PubMed:19933331};
AltName: Full=Cholest-4-en-3-one C26-monooxygenase {ECO:0000303|PubMed:20843794};
AltName: Full=Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] {ECO:0000303|PubMed:20843794};
AltName: Full=Cholesterol C26-monooxygenase {ECO:0000303|PubMed:20843794};
AltName: Full=Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming] {ECO:0000303|PubMed:20843794};
AltName: Full=Cytochrome P450 124 {ECO:0000303|PubMed:19933331};
AltName: Full=Steroid C26-monooxygenase {ECO:0000303|PubMed:20843794};
EC=1.14.13.221 {ECO:0000269|PubMed:20843794};
AltName: Full=Steroid C27-monooxygenase {ECO:0000303|PubMed:20843794};
Name=cyp124; OrderedLocusNames=Rv2266; ORFNames=MTCY339.44c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
AND SUBSTRATE SPECIFICITY.
PubMed=20843794; DOI=10.1074/jbc.M110.161117;
Johnston J.B., Ouellet H., Ortiz de Montellano P.R.;
"Functional redundancy of steroid C26-monooxygenase activity in
Mycobacterium tuberculosis revealed by biochemical and genetic
analyses.";
J. Biol. Chem. 285:36352-36360(2010).
[3]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH
(3R,7S,11S)-3,7,11,15-TETRAMETHYLHEXADECANOIC ACID (PHYTANIC ACID) AND
HEME, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=H37Rv;
PubMed=19933331; DOI=10.1073/pnas.0907398106;
Johnston J.B., Kells P.M., Podust L.M., Ortiz de Montellano P.R.;
"Biochemical and structural characterization of CYP124: a methyl-
branched lipid omega-hydroxylase from Mycobacterium tuberculosis.";
Proc. Natl. Acad. Sci. U.S.A. 106:20687-20692(2009).
-!- FUNCTION: Primarily hydroxylates the omega-carbon of a number of
methyl-branched lipids, including (2E,6E)-farnesol, phytanate,
geranylgeraniol, 15-methylpalmitate and (2E,6E)-farnesyl
diphosphate (PubMed:19933331). Also catalyzes the sequential
oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-
26-hydroxycholest-4-en-3-one (alcohol), (25R)-26-oxocholest-4-en-
3-one (aldehyde), to finally yield the carboxylic acid (25R)-3-
oxocholest-4-en-26-oate (PubMed:20843794). Cyp124 catalyzes
preferencially the oxidation of (25R)-26-hydroxycholest-4-en-3-one
diastereomer (PubMed:20843794). Also able to sequentially oxidize
cholesterol itself, not only cholest-4-en-3-one (PubMed:20843794).
{ECO:0000269|PubMed:19933331, ECO:0000269|PubMed:20843794}.
-!- CATALYTIC ACTIVITY: A methyl-branched lipid + O(2) + 2 reduced
ferredoxin [iron-sulfur] cluster + 2 H(+) = an omega-hydroxy-
methyl-branched lipid + H(2)O + 2 oxidized ferredoxin [iron-
sulfur] cluster. {ECO:0000269|PubMed:19933331}.
-!- CATALYTIC ACTIVITY: Cholest-4-en-3-one + 3 NADPH + 3 O(2) = (25R)-
3-oxocholest-4-en-26-oate + 3 NADP(+) + 4 H(2)O.
{ECO:0000269|PubMed:20843794}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:19933331,
ECO:0000269|PubMed:20843794};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=9 uM for 15-methylpalmitate {ECO:0000269|PubMed:19933331};
KM=11.6 uM for cholesterol {ECO:0000269|PubMed:20843794};
KM=20.8 uM for cholest-4-en-3-one {ECO:0000269|PubMed:20843794};
KM=54 uM for phytanate {ECO:0000269|PubMed:19933331};
KM=36 uM for (2E,6E)-farnesol {ECO:0000269|PubMed:19933331};
KM=32 uM for geranylgeraniol {ECO:0000269|PubMed:19933331};
Note=Kcat is 11.7 min(-1) for cholesterol as substrate. Kcat is
1.5 min(-1) for cholest-4-en-3-one as substrate.
{ECO:0000269|PubMed:20843794};
-!- PATHWAY: Lipid metabolism; branched-chain fatty acid metabolism.
{ECO:0000305|PubMed:19933331}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AL123456; CCP45047.1; -; Genomic_DNA.
PIR; F70729; F70729.
RefSeq; NP_216782.1; NC_000962.3.
RefSeq; WP_003411654.1; NZ_KK339370.1.
PDB; 2WM4; X-ray; 2.11 A; A=1-428.
PDB; 2WM5; X-ray; 1.50 A; A=1-428.
PDBsum; 2WM4; -.
PDBsum; 2WM5; -.
ProteinModelPortal; P9WPP3; -.
SMR; P9WPP3; -.
STRING; 83332.Rv2266; -.
SwissLipids; SLP:000001010; -.
PaxDb; P9WPP3; -.
EnsemblBacteria; CCP45047; CCP45047; Rv2266.
GeneID; 887763; -.
KEGG; mtu:Rv2266; -.
TubercuList; Rv2266; -.
eggNOG; ENOG4106A3M; Bacteria.
eggNOG; COG2124; LUCA.
KO; K20497; -.
OMA; IHRCVGM; -.
PhylomeDB; P9WPP3; -.
BioCyc; MetaCyc:G185E-6483-MONOMER; -.
UniPathway; UPA01022; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0036199; F:cholest-4-en-3-one 26-monooxygenase activity; IDA:UniProtKB.
GO; GO:0031073; F:cholesterol 26-hydroxylase activity; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
GO; GO:0006707; P:cholesterol catabolic process; IBA:GO_Central.
GO; GO:0010430; P:fatty acid omega-oxidation; IDA:MTBBASE.
GO; GO:0097089; P:methyl-branched fatty acid metabolic process; IDA:MTBBASE.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR002397; Cyt_P450_B.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 2.
PRINTS; PR00359; BP450.
SUPFAM; SSF48264; SSF48264; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Fatty acid metabolism; Heme; Iron;
Lipid metabolism; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
Reference proteome.
CHAIN 1 428 Methyl-branched lipid omega-hydroxylase.
/FTId=PRO_0000052278.
METAL 379 379 Iron (heme axial ligand).
{ECO:0000244|PDB:2WM4,
ECO:0000244|PDB:2WM5,
ECO:0000269|PubMed:19933331}.
HELIX 21 23 {ECO:0000244|PDB:2WM5}.
HELIX 29 32 {ECO:0000244|PDB:2WM5}.
HELIX 36 49 {ECO:0000244|PDB:2WM5}.
STRAND 51 55 {ECO:0000244|PDB:2WM5}.
STRAND 69 72 {ECO:0000244|PDB:2WM5}.
HELIX 75 83 {ECO:0000244|PDB:2WM5}.
TURN 85 87 {ECO:0000244|PDB:2WM5}.
STRAND 95 97 {ECO:0000244|PDB:2WM5}.
HELIX 101 108 {ECO:0000244|PDB:2WM5}.
HELIX 109 112 {ECO:0000244|PDB:2WM5}.
HELIX 117 127 {ECO:0000244|PDB:2WM5}.
HELIX 131 155 {ECO:0000244|PDB:2WM5}.
STRAND 159 162 {ECO:0000244|PDB:2WM5}.
HELIX 163 166 {ECO:0000244|PDB:2WM5}.
TURN 167 169 {ECO:0000244|PDB:2WM5}.
HELIX 170 180 {ECO:0000244|PDB:2WM5}.
HELIX 184 186 {ECO:0000244|PDB:2WM5}.
HELIX 187 199 {ECO:0000244|PDB:2WM5}.
TURN 203 205 {ECO:0000244|PDB:2WM4}.
HELIX 209 232 {ECO:0000244|PDB:2WM5}.
HELIX 238 244 {ECO:0000244|PDB:2WM5}.
STRAND 246 251 {ECO:0000244|PDB:2WM4}.
HELIX 254 267 {ECO:0000244|PDB:2WM5}.
HELIX 270 285 {ECO:0000244|PDB:2WM5}.
HELIX 287 295 {ECO:0000244|PDB:2WM5}.
HELIX 297 312 {ECO:0000244|PDB:2WM5}.
STRAND 318 324 {ECO:0000244|PDB:2WM5}.
STRAND 326 328 {ECO:0000244|PDB:2WM5}.
STRAND 331 333 {ECO:0000244|PDB:2WM5}.
STRAND 338 341 {ECO:0000244|PDB:2WM5}.
HELIX 343 346 {ECO:0000244|PDB:2WM5}.
TURN 350 352 {ECO:0000244|PDB:2WM5}.
STRAND 353 355 {ECO:0000244|PDB:2WM5}.
STRAND 373 375 {ECO:0000244|PDB:2WM5}.
HELIX 382 399 {ECO:0000244|PDB:2WM5}.
STRAND 404 407 {ECO:0000244|PDB:2WM4}.
STRAND 415 417 {ECO:0000244|PDB:2WM5}.
STRAND 420 422 {ECO:0000244|PDB:2WM5}.
STRAND 424 426 {ECO:0000244|PDB:2WM5}.
SEQUENCE 428 AA; 47825 MW; 76B1F3C5AE348591 CRC64;
MGLNTAIATR VNGTPPPEVP IADIELGSLD FWALDDDVRD GAFATLRREA PISFWPTIEL
PGFVAGNGHW ALTKYDDVFY ASRHPDIFSS YPNITINDQT PELAEYFGSM IVLDDPRHQR
LRSIVSRAFT PKVVARIEAA VRDRAHRLVS SMIANNPDRQ ADLVSELAGP LPLQIICDMM
GIPKADHQRI FHWTNVILGF GDPDLATDFD EFMQVSADIG AYATALAEDR RVNHHDDLTS
SLVEAEVDGE RLSSREIASF FILLVVAGNE TTRNAITHGV LALSRYPEQR DRWWSDFDGL
APTAVEEIVR WASPVVYMRR TLTQDIELRG TKMAAGDKVS LWYCSANRDE SKFADPWTFD
LARNPNPHLG FGGGGAHFCL GANLARREIR VAFDELRRQM PDVVATEEPA RLLSQFIHGI
KTLPVTWS


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