CP52M_STABO
ID CP52M_STABO Reviewed; 538 AA.
AC B8QHP1;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Cytochrome P450 52-M1 {ECO:0000305};
DE Short=CYP52-M1;
DE EC=1.14.14.80 {ECO:0000269|PubMed:23516968, ECO:0000269|PubMed:24242247};
DE AltName: Full=Cytochrome P450 monooxygenase CYP52-M1 {ECO:0000303|PubMed:19054129};
GN Name=cyp52M1 {ECO:0000303|PubMed:19054129};
OS Starmerella bombicola (Yeast) (Candida bombicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Starmerella.
OX NCBI_TaxID=75736;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 22214 / CBS 6009 / JCM 9596 / NBRC 10243 / NRRL Y-17069;
RX PubMed=19054129; DOI=10.1111/j.1567-1364.2008.00454.x;
RA van Bogaert I.N., Demey M., Develter D., Soetaert W., Vandamme E.J.;
RT "Importance of the cytochrome P450 monooxygenase CYP52 family for the
RT sophorolipid-producing yeast Candida bombicola.";
RL FEMS Yeast Res. 9:87-94(2009).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC STRAIN=ATCC 22214 / CBS 6009 / JCM 9596 / NBRC 10243 / NRRL Y-17069;
RX PubMed=23964782; DOI=10.1021/pr400392a;
RA Ciesielska K., Li B., Groeneboer S., Van Bogaert I., Lin Y.C., Soetaert W.,
RA Van de Peer Y., Devreese B.;
RT "SILAC-based proteome analysis of Starmerella bombicola sophorolipid
RT production.";
RL J. Proteome Res. 12:4376-4392(2013).
RN [3]
RP FUNCTION.
RX PubMed=23516968; DOI=10.1111/mmi.12200;
RA Van Bogaert I.N., Holvoet K., Roelants S.L., Li B., Lin Y.C.,
RA Van de Peer Y., Soetaert W.;
RT "The biosynthetic gene cluster for sophorolipids: a biotechnological
RT interesting biosurfactant produced by Starmerella bombicola.";
RL Mol. Microbiol. 88:501-509(2013).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=24242247; DOI=10.1128/aem.02886-13;
RA Huang F.C., Peter A., Schwab W.;
RT "Expression and characterization of CYP52 genes involved in the
RT biosynthesis of sophorolipid and alkane metabolism from Starmerella
RT bombicola.";
RL Appl. Environ. Microbiol. 80:766-776(2014).
CC -!- FUNCTION: Catalyzes the first step of sophorolipid biosynthesis.
CC Catalyzes the terminal (at the omega-position) or subterminal (at the
CC omega(-1)-position) hydroxylation of a fatty acid. This converts the
CC fatty acid to a substrate for the subsequent glycosyltransferase
CC reactions (PubMed:23516968, PubMed:24242247). Oleic acid is the
CC preferred substrate, but it acts on various other C-16, C-18 and C-20
CC saturated and unsaturated fatty acids, namely palmitic, palmitoleic,
CC stearic, linoleic, cis-9,10-epoxystearic, trans-9,10-epoxystearic and
CC arachidonic acid (PubMed:24242247). {ECO:0000269|PubMed:23516968,
CC ECO:0000269|PubMed:24242247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--
CC hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:140991,
CC ChEBI:CHEBI:140992; EC=1.14.14.80;
CC Evidence={ECO:0000269|PubMed:23516968, ECO:0000269|PubMed:24242247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (omega-1)-ethyl fatty acid + O2 + reduced [NADPH--
CC hemoprotein reductase] = an (omega-1)-hydroxy-long-chain fatty acid +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:60936, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:84493,
CC ChEBI:CHEBI:144045; Evidence={ECO:0000269|PubMed:23516968,
CC ECO:0000269|PubMed:24242247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 18-hydroxy-(9Z)-octadecenoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:41728, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78424;
CC EC=1.14.14.80; Evidence={ECO:0000269|PubMed:24242247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 17-hydroxy-(9Z)-octadecenoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60928, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:144040;
CC Evidence={ECO:0000269|PubMed:24242247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 18-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60580,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132029;
CC Evidence={ECO:0000269|PubMed:24242247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 17-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60932,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:144041;
CC Evidence={ECO:0000269|PubMed:24242247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC 16-hydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:40199, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:55329, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.80;
CC Evidence={ECO:0000269|PubMed:24242247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = (9Z)-16-hydroxyhexadec-9-enoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60940, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:144048;
CC Evidence={ECO:0000269|PubMed:24242247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + octadecanoate + reduced [NADPH--hemoprotein reductase] =
CC 18-hydroxyoctadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:46356, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:86046; EC=1.14.14.80;
CC Evidence={ECO:0000269|PubMed:24242247};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for oleic acid {ECO:0000269|PubMed:24242247};
CC KM=68 uM for linoleic acid {ECO:0000269|PubMed:24242247};
CC KM=54 uM for arachidonic acid {ECO:0000269|PubMed:24242247};
CC Vmax=535 pmol/min/mg enzyme for oleic acid
CC {ECO:0000269|PubMed:24242247};
CC Vmax=451 pmol/min/mg enzyme for linoleic acid
CC {ECO:0000269|PubMed:24242247};
CC Vmax=306 pmol/min/mg enzyme for arachidonic acid
CC {ECO:0000269|PubMed:24242247};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:24242247};
CC Temperature dependence:
CC Optimum temperature is 25-30 degrees Celsius.
CC {ECO:0000269|PubMed:24242247};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Only expressed in stationary phase.
CC {ECO:0000269|PubMed:19054129, ECO:0000269|PubMed:23964782}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; EU552419; ACD75398.1; -; Genomic_DNA.
DR AlphaFoldDB; B8QHP1; -.
DR SMR; B8QHP1; -.
DR KEGG; ag:ACD75398; -.
DR BioCyc; MetaCyc:MON-18770; -.
DR BRENDA; 1.14.14.80; 1101.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0120319; F:long-chain fatty acid omega-1 hydroxylase activity; IEA:RHEA.
DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; IEA:UniProtKB-EC.
DR 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; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002974; Cyt_P450_E_CYP52.
DR InterPro; IPR002402; Cyt_P450_E_grp-II.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00464; EP450II.
DR PRINTS; PR01239; EP450IICYP52.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..538
FT /note="Cytochrome P450 52-M1"
FT /id="PRO_0000443096"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 484
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:P04798"
SQ SEQUENCE 538 AA; 61841 MW; 09D5B77A76F58479 CRC64;
MLIKDIILTP MSLSAVAGLL PLLFVAFLVL HEPIWLLWYR YAARRHKCSM PRFIEKSFPL
GIQRTMDMIK TAKSYTLLEV QYDRVFNKFK ARTYLRQAPL QYQIFTIEPE NIKTILATKF
NDFGLGARFH TVGKVFGQGI FTLSGNGWKQ SRSMLRPQFT KDQVCRIDQI SSHAAELIKE
MNRAMKVDQF IDVQHYFHKL TLDTATEFLF GESCESLNPE NQSCIVARDG SEITAEQFVE
SYNFLLNYAF KRTLSSKVYW LFNSKEFRDH KKRAQSYIDY YVDKALYATS FAAENSIAEK
DAAAESSGIY VFSLEMAKVT RDPVTIRDQI FNILIAGRDT TAATLSFAIH FLARNPDVFN
KLREEVLDHF GTKEEQRPLS FELLKQAPYL KQVINEVLRL APVLPLNFRT AVRDTTLPIG
GGPEQKDPIF VPKGTAVYYS IYMVHRDIKY WGPDAHEFNP NRWENLKLDN VWAFLPFNGG
PRICLGQQFA LTELSLTLVR LLQEYSKIEM GPDFPESPRF STTLTAQHAP PGVVVRFS
