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Database: UniProt
Entry: H1V9Q4_COLHI
LinkDB: H1V9Q4_COLHI
Original site: H1V9Q4_COLHI 
ID   H1V9Q4_COLHI            Unreviewed;       486 AA.
AC   H1V9Q4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Ent-kaurene oxidase {ECO:0000313|EMBL:CCF36957.1};
GN   ORFNames=CH063_01606 {ECO:0000313|EMBL:CCF36957.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF36957.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; CACQ02002234; CCF36957.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1V9Q4; -.
DR   STRING; 759273.H1V9Q4; -.
DR   EnsemblFungi; CCF36957; CCF36957; CH063_01606.
DR   VEuPathDB; FungiDB:CH63R_03638; -.
DR   eggNOG; KOG0684; Eukaryota.
DR   HOGENOM; CLU_022195_0_0_1; -.
DR   Proteomes; UP000007174; 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:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11041; CYP503A1-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR46206; CYTOCHROME P450; 1.
DR   PANTHER; PTHR46206:SF7; ENT-KAURENE OXIDASE; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..486
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003555070"
FT   BINDING         427
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:PIRSR602403-1"
SQ   SEQUENCE   486 AA;  53745 MW;  E6F3A6C887363F25 CRC64;
     MSSRLPVLSS SLIFLLAAVL AQPFFKADPL AHIPVVGKGG KEARRKQYVS GGSESIVVAP
     KYMPELRRLP DDILSFTEAS NESLQSEYTH MNSDAPGLPQ IVKSMLTPAL VRLNPIISTE
     VAETMASELP QSGEWEEVDI NQKLLRIVAI VSGRIFVGPE LCRNETYIDS AINYTIDVMV
     AVYMIGLVPV WLRPFLAPRL PFVKKLEKRI QEADDFLRPV VKERRTAMQD PSLASHDDML
     QWIINSEIKR GNVDDKAVAK LQLSVSMAAI HTTTLTALNA LYTLAAMPHL VPELRDEIRQ
     ALKDNDGEFG SPALQSMKKL DSFLKETMRC FPLSAVSFQR KVLKPFALSN GQTIPAGVIV
     EVPAGSIAAD GAIFDNPGEF DHLRYYKMRQ SKGSQATGSA KAEVVANSQF VSVSESSLTF
     GYGRHACPGR FFAANEIKMI MANILLHYEI RNPDGVTERH KNVRTGSQLS PDHTKRVMIK
     KIQGDI
//
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