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Entry: M2SJH8_COCSN
LinkDB: M2SJH8_COCSN
Original site: M2SJH8_COCSN 
ID   M2SJH8_COCSN            Unreviewed;       535 AA.
AC   M2SJH8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=sterol 22-desaturase {ECO:0000256|ARBA:ARBA00039038};
DE            EC=1.14.19.41 {ECO:0000256|ARBA:ARBA00039038};
GN   ORFNames=COCSADRAFT_221542 {ECO:0000313|EMBL:EMD62495.1};
OS   Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS   spot blotch fungus) (Bipolaris sorokiniana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD62495.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD62495.1, ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445646; EMD62495.1; -; Genomic_DNA.
DR   RefSeq; XP_007701852.1; XM_007703662.1.
DR   AlphaFoldDB; M2SJH8; -.
DR   STRING; 665912.M2SJH8; -.
DR   GeneID; 19134595; -.
DR   KEGG; bsc:COCSADRAFT_221542; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_023517_0_0_1; -.
DR   OMA; MVIPSFY; -.
DR   OrthoDB; 5393233at2759; -.
DR   Proteomes; UP000016934; 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; cd11082; CYP61_CYP710; 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; PTHR24286:SF228; C-22 STEROL DESATURASE ERG5; 1.
DR   PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
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: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|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016934}.
FT   BINDING         479
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   535 AA;  60871 MW;  FE2421E1F72061B4 CRC64;
     MAANVSFVSP TADAKAAQVL QDFDTSGLLS SVVTGLTVWK LALTLIVTAV AYDQFKYIWN
     KGSIVGPSWK IPFIGPFLES VNPDFNKYHE KWSSGPLSCV SVFHKFVVIA STRDMARKIF
     NSPSFVKPCV VDVAYKLLRP ENWVFLDGRA HVDYRKGLNS LFTRQALEQY LPGQEDIYNK
     YFKQFVHLSQ VENKGKHVPW MQEFRLMITA LSCRTFVGHY CSDEAVKKIA DDYYLITAAL
     ELVNFPIIIP FTKTWYGKKC ADMVLDEFSK CAAKSKVRMA AGGKKECILD FWVDNMIQSE
     KYRKRVEAGE KVDDSEKPAT VIRWFSDIEI SMTIFTFLFA SQDATSSAAT WLFQIMADRP
     EYLGKIREEN IKARNGDVHA SLSLDAIEKL QWTRAIVKET LRYRPPVIMV PYLAKKDFPV
     TPDYTVPKGS MVIPTTYMAL HDPEAYPNPE SFEPERWITG DADQQTKNWL VFGTGPHYCL
     GQTYAQANLM LMIGKASMLL DWDHKVTDQS EVIKVFATIF PMDDCLLTFK DRVAA
//
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