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Database: UniProt
Entry: G4ZRU8_PHYSP
LinkDB: G4ZRU8_PHYSP
Original site: G4ZRU8_PHYSP 
ID   G4ZRU8_PHYSP            Unreviewed;       313 AA.
AC   G4ZRU8;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Fatty acid desaturase domain-containing protein {ECO:0000259|Pfam:PF00487};
GN   ORFNames=PHYSODRAFT_547344 {ECO:0000313|EMBL:EGZ13985.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ13985.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ13985.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ13985.1,
RC   ECO:0000313|Proteomes:UP000002640};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|RuleBase:RU000581};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC       metal ions. {ECO:0000256|RuleBase:RU000581}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00009295, ECO:0000256|RuleBase:RU000581}.
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DR   EMBL; JH159156; EGZ13985.1; -; Genomic_DNA.
DR   RefSeq; XP_009531414.1; XM_009533119.1.
DR   AlphaFoldDB; G4ZRU8; -.
DR   STRING; 1094619.G4ZRU8; -.
DR   EnsemblProtists; EGZ13985; EGZ13985; PHYSODRAFT_547344.
DR   GeneID; 20662625; -.
DR   KEGG; psoj:PHYSODRAFT_547344; -.
DR   InParanoid; G4ZRU8; -.
DR   OMA; IGYHRLY; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03505; Delta9-FADS-like; 1.
DR   InterPro; IPR015876; Acyl-CoA_DS.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR   PANTHER; PTHR11351:SF98; FA_DESATURASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   PRINTS; PR00075; FACDDSATRASE.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU000581};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU000581};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000581};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002640};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000581};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        40..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          43..245
FT                   /note="Fatty acid desaturase"
FT                   /evidence="ECO:0000259|Pfam:PF00487"
SQ   SEQUENCE   313 AA;  36299 MW;  0AC38D6B0D44195F CRC64;
     MMSLSKFKKE ANWFMVYYLT VVHLGAIEGL RRLFQCKLET FPLFVFIYYL SGLGITMGAH
     RLWAHRSYKA HGILRFFLML CNSMANQGTL FHWSRDHRVH HKYSDTVADP HDSGRGFFFA
     HMGWLLVKKD PRVLEAGTKL NYDDLWADWC VVMQEKLNPW GQLFMCFVFP TIVGVQAVGE
     DWKNALFILG FLRYVAVLHA TWLVNSAAHF YGYQTYDNIP PRENWFVSIW AIGEGWHNWH
     HKFPYDYAAS EFGISGQFNP TKLTIDCMAL LGLVSDRKRA TDIWAKIKDS KSFQDPNGDD
     PTKAFSELKA KAN
//
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