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Database: UniProt
Entry: A0A0J9UR52_FUSO4
LinkDB: A0A0J9UR52_FUSO4
Original site: A0A0J9UR52_FUSO4 
ID   A0A0J9UR52_FUSO4        Unreviewed;       537 AA.
AC   A0A0J9UR52;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=sterol 22-desaturase {ECO:0000256|ARBA:ARBA00039038};
DE            EC=1.14.19.41 {ECO:0000256|ARBA:ARBA00039038};
GN   ORFNames=FOXG_04166 {ECO:0000313|EMBL:KNB00671.1};
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS   / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428 {ECO:0000313|EMBL:KNB00671.1, ECO:0000313|Proteomes:UP000009097};
RN   [1] {ECO:0000313|EMBL:KNB00671.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB00671.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA   Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA   Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA   Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA   Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KNB00671.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB00671.1};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA   Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA   Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA   Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA   Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
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; DS231699; KNB00671.1; -; Genomic_DNA.
DR   RefSeq; XP_018238716.1; XM_018382068.1.
DR   AlphaFoldDB; A0A0J9UR52; -.
DR   GeneID; 28946230; -.
DR   KEGG; fox:FOXG_04166; -.
DR   VEuPathDB; FungiDB:FOXG_04166; -.
DR   OrthoDB; 5393233at2759; -.
DR   Proteomes; UP000009097; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009097}.
FT   BINDING         481
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   537 AA;  60448 MW;  E7A1B9639275C6DA CRC64;
     MEAVNATSSG FSSVLAGTKY ANVALPPQVE YVIEAVSNAG VWTWVFTFIA LCVAYDQIAY
     IIRKGPIEGP AMKLPFIGPF LDSMDPRFDG YHAKWSSGPL SCVSIFHKFV VIASTRDMAR
     KVFNSPAYVK PTVVDVAPKL LGHDNWVFLD GKAHVDFRKG LNGLFTRKAL ESYLPGQEEA
     YNTYFKHFLK MTKDAGGKPV PFMHEFREVM CAVSCRTFVG HYISDEAVTK IAEDYYLITA
     ALELVNLPVI LPYTKSWYGK KAADMVLAEF SKCAAKSKVR MAAGGEVTCI MDAWVLSMIQ
     SERWREAEEK GEGHTVEKPT PLLRMFNDYE ISQTIFTFLF ASQDATSSAA TWLFQVTAQR
     PDVLDRVREE NIKVRNGDPN APITMDQLES LTYTRAVVRE LLRWRPPVIM VPYVTKKAFP
     LTENYTVPKG SMLIPTTFMA LHDPEVYDNP SHFDPERYYS GDAEEKGSKN YLVFGTGPHY
     CLGQVYAQLN LALMIGKASV MLDWKHHATP KSEEIKVFAT IFPMVCTRYR AIQCNND
//
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