CP124_MYCTO
ID CP124_MYCTO Reviewed; 428 AA.
AC P9WPP2; L0TBS5; P0A516; Q50696;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Methyl-branched lipid omega-hydroxylase {ECO:0000250|UniProtKB:P9WPP3};
DE EC=1.14.15.14 {ECO:0000250|UniProtKB:P9WPP3};
DE AltName: Full=Cholest-4-en-3-one C26-monooxygenase {ECO:0000250|UniProtKB:P9WPP3};
DE AltName: Full=Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] {ECO:0000250|UniProtKB:P9WPP3};
DE AltName: Full=Cholesterol C26-monooxygenase {ECO:0000250|UniProtKB:P9WPP3};
DE AltName: Full=Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming] {ECO:0000250|UniProtKB:P9WPP3};
DE AltName: Full=Cytochrome P450 124 {ECO:0000250|UniProtKB:P9WPP3};
DE AltName: Full=Steroid C26-monooxygenase {ECO:0000250|UniProtKB:P9WPP3};
DE EC=1.14.15.28 {ECO:0000250|UniProtKB:P9WPP3};
DE AltName: Full=Steroid C27-monooxygenase {ECO:0000250|UniProtKB:P9WPP3};
GN Name=cyp124; OrderedLocusNames=MT2328;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Primarily hydroxylates the omega-carbon of a number of
CC methyl-branched lipids, including (2E,6E)-farnesol, phytanate,
CC geranylgeraniol, 15-methylpalmitate and (2E,6E)-farnesyl diphosphate.
CC Also catalyzes the sequential oxidation of the terminal methyl of
CC cholest-4-en-3-one into (25R)-26-hydroxycholest-4-en-3-one (alcohol),
CC (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the
CC carboxylic acid (25R)-3-oxocholest-4-en-26-oate. Also able to
CC sequentially oxidize cholesterol itself, not only cholest-4-en-3-one.
CC {ECO:0000250|UniProtKB:P9WPP3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a methyl-branched lipid + O2 + 2 reduced ferredoxin [iron-
CC sulfur] cluster + 2 H(+) = an omega-hydroxy-methyl-branched lipid +
CC H2O + 2 oxidized ferredoxin [iron-sulfur] cluster.; EC=1.14.15.14;
CC Evidence={ECO:0000250|UniProtKB:P9WPP3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholest-4-en-3-one + 5 H(+) + 3 O2 + 6 reduced [2Fe-2S]-
CC [ferredoxin] = (25R)-3-oxocholest-4-en-26-oate + 4 H2O + 6 oxidized
CC [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:49996, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16175, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:71570; EC=1.14.15.28;
CC Evidence={ECO:0000250|UniProtKB:P9WPP3};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P9WPP3};
CC -!- PATHWAY: Lipid metabolism; branched-chain fatty acid metabolism.
CC {ECO:0000250|UniProtKB:P9WPP3}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46610.1; -; Genomic_DNA.
DR PIR; F70729; F70729.
DR RefSeq; WP_003917608.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPP2; -.
DR SMR; P9WPP2; -.
DR EnsemblBacteria; AAK46610; AAK46610; MT2328.
DR KEGG; mtc:MT2328; -.
DR PATRIC; fig|83331.31.peg.2503; -.
DR HOGENOM; CLU_033716_0_0_11; -.
DR UniPathway; UPA01022; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0036199; F:cholest-4-en-3-one 26-monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0031073; F:cholesterol 26-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0070402; F:NADPH binding; ISS:UniProtKB.
DR GO; GO:0010430; P:fatty acid omega-oxidation; ISS:UniProtKB.
DR GO; GO:0097089; P:methyl-branched fatty acid metabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 2.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism; Heme; Iron; Lipid metabolism; Metal-binding;
KW Monooxygenase; NADP; Oxidoreductase.
FT CHAIN 1..428
FT /note="Methyl-branched lipid omega-hydroxylase"
FT /id="PRO_0000426917"
FT BINDING 379
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P9WPP3"
SQ SEQUENCE 428 AA; 47718 MW; 3411C978BBD1A37F CRC64;
MGLNTAIATR VNGTPPPEVP IAGIELGSLD FWALDDDVRD GAFATLRREA PISFWPTIEL
PGFVAGNGHW ALTKNDDVFY 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
