CP52E_STABO
ID CP52E_STABO Reviewed; 519 AA.
AC B8QHP3;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Cytochrome P450 52-E3 {ECO:0000305};
DE Short=CYP52-E3;
DE EC=1.14.14.80 {ECO:0000269|PubMed:24242247};
DE AltName: Full=Cytochrome P450 monooxygenase CYP52-E3 {ECO:0000303|PubMed:19054129};
GN Name=cyp52E3 {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 FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE 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 terminal (at the omega-position) hydroxylation
CC of a fatty acid. Probably involved in alkane metabolism. Has minor
CC activity toward myristic acid, palmitic acid, palmitoleic acid and
CC oleic acid. {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: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=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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Up-regulated when grown on alkanes as sole carbon source.
CC {ECO:0000269|PubMed:19054129}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; EU552420; ACD75400.1; -; Genomic_DNA.
DR AlphaFoldDB; B8QHP3; -.
DR SMR; B8QHP3; -.
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: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..519
FT /note="Cytochrome P450 52-E3"
FT /id="PRO_0000447696"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 461
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 519 AA; 58940 MW; 89C5AE628C5BAF42 CRC64;
MNINFSDVLV LGGISVSFLL AYQAIYFYFI YSPRAKKLGC ALPPVFFSFP LGIPEVIRLV
NAWFNDDLLE YFTFKFEEFQ RKTGFQSVAG QLWIGTIEPE NIKTMLATSF KDYSLGFRYE
AMYGLLGNGI FTLSGEGWKH SRALLRPQFS REQVSHLESM RTHINMLINN HFKGGKVVDA
QVLFHNLTID TATEFLFGES TNTLDPALAQ HGFPGPKGLV TGEQFAEAFT SALELLSVRV
MAGAAWFLVW TPKFWRSCKV CHNFIDYFVF KALATPMEKD QEADRYVFIR ELTKETSDPR
VIRDQALNIL LAGRDTTAAL LSFTTYYLGA YPEVYDELRE AVIADFGKED AEPPTFEQLK
QCKVLQNVIR EVLRLHPNVP LNFREAITDT KFPTGGGPNG DQPVFVPKGQ KVFYATYVMQ
RNEGLWGPDS TTFRPDRWNE SREAIASGWD YIPFNGGPRI CLGQQFALTE ASYTLVRICQ
EFSRIEVLHP DVITSRNVMK QRMRLTNSSS GGVIAKFIR
