ID A7F790_SCLS1 Unreviewed; 522 AA.
AC A7F790;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Cytochrome P450 alkane hydroxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SS1G_13470 {ECO:0000313|EMBL:EDN98611.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN98611.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602402-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CH476645; EDN98611.1; -; Genomic_DNA.
DR RefSeq; XP_001585586.1; XM_001585536.1.
DR AlphaFoldDB; A7F790; -.
DR STRING; 665079.A7F790; -.
DR EnsemblFungi; EDN98611; EDN98611; SS1G_13470.
DR GeneID; 5481722; -.
DR KEGG; ssl:SS1G_13470; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_0_1; -.
DR InParanoid; A7F790; -.
DR OMA; AKNPRIW; -.
DR OrthoDB; 4950799at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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 CDD; cd11063; CYP52; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002974; Cyt_P450_E_CYP52_ascomycetes.
DR InterPro; IPR047146; Cyt_P450_E_CYP52_fungi.
DR InterPro; IPR002402; Cyt_P450_E_grp-II.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24287; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR24287:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 2.
DR PRINTS; PR00464; EP450II.
DR PRINTS; PR01239; EP450IICYP52.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602402-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|PIRSR:PIRSR602402-1, ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602402-1,
KW ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..522
FT /note="Cytochrome P450 alkane hydroxylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002708154"
FT BINDING 467
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:0000256|PIRSR:PIRSR602402-1"
SQ SEQUENCE 522 AA; 59310 MW; 4C4A88E10941BBD5 CRC64;
MAYYGLSFIL IVAAFLVHKI TNHVSARRFQ KAHCCKPVHK LPQRERIIGW DMYKFQVKSA
KEKRRLKAGY DRYKENGNTY VLSMMGFDFF NTIEPENLKT LLAVNFKDYD LGARRGAFSP
LLGDGIFTTD GAQWEHSRAL VRPNFNKSQV ADLNIFEKHI QVLLSQIPRD GSTFDLQSLF
FKLTLDTATE FLFGKSVHSL TSIEGSEQQK FGAAFDLGQI KLEVRFTMGK LSNWMCDSEF
DEACKTVHSF VDKIVYEALS KIDAKEEKAV EGHGPGRYVF LTEMVKASRD PKQLRDELLN
ILLAGRDTTA SLLSNTFHIL ARRPDIWEKL KAEVDELHGE RPDYETMKGM KYIKYVLNEC
KCLSLSSSIM ASLTTGLKAL RLYPVVPSNA RFSRRDTVLP VGGGPDRTSP IFIPKGSAVA
WSTYSMHRRT DIFGPDAEEF RPERWAPEEG LRPGWGYLPF NGGPRICVGQ QFALAEASYT
IIRLLQEFDR ILDRDGTEWK EQFALTACSA KGVQVGMIPR RM
//
