CP52N_STABO
ID CP52N_STABO Reviewed; 523 AA.
AC B8QHP5;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Cytochrome P450 52-N1 {ECO:0000305};
DE Short=CYP52-N1;
DE EC=1.14.14.80 {ECO:0000269|PubMed:24242247};
DE AltName: Full=Cytochrome P450 monooxygenase CYP52-N1 {ECO:0000303|PubMed:19054129};
GN Name=cyp52N1 {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. Linoleic acid
CC is the preferred substrate, but it acts on various other C-16, C-18 and
CC C-20 saturated and unsaturated fatty acids, namely palmitic,
CC palmitoleic, stearic, oleic, alpha-linoleic, arachidonic and myristic
CC 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,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)-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 -!- 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 -!- 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; EU552421; ACD75402.1; -; Genomic_DNA.
DR AlphaFoldDB; B8QHP5; -.
DR SMR; B8QHP5; -.
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..523
FT /note="Cytochrome P450 52-N1"
FT /id="PRO_0000447697"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 469
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 523 AA; 59596 MW; 1987EDDCA7A35705 CRC64;
MILYAVLGAF AAFLLYMDVL YPFVIYPLRA RWHKCGYIPR DLSWPLGIPL TLVVLSKLRK
DMLLQFMAAQ DLSRPYKTSL RQFLGKWVIA TRDPENIKAV LSTKFNDFSL KERGNRMRHV
IGDGIFTQDG APWKHSRDML RPQFTKDQIS RVELLSHHID VLIREIRKSG GNVELQRLFH
LMTMDTATHF LFGESVGSLE VSGESKGIEI TDPKTGEIVN TVDFVESYTF ANKFALKKII
LNDLEFLADL TEPSYKWHLR RVHTVMDHYV QLALKATEKY DPDDDSEKGE YYFSHELAKL
TRDPLSLRDQ LFNILIAGRD TTAATLSYAF HYLTKNPAIY AKVREDVLTV FPNGDASLAT
YEDLRKAKYL QMVIKEVLRL APAVPLNTRA AVRDTYLPRG GGPAGNLPVF VPKGTAVNYP
TYILHRDPDI YGADAYEFNP ERWRPENKLP NSPMYSWGYI PFNGGPRICI GQQFALTEIA
LTMIKLVLEF ERLEPADDFE PNLQDKSSLT VMVGGSGVRV KLS
