ID A0A093PIZ7_9PASS Unreviewed; 354 AA.
AC A0A093PIZ7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=stearoyl-CoA 9-desaturase {ECO:0000256|ARBA:ARBA00012620};
DE EC=1.14.19.1 {ECO:0000256|ARBA:ARBA00012620};
DE Flags: Fragment;
GN ORFNames=N305_07131 {ECO:0000313|EMBL:KFW76833.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW76833.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW76833.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW76833.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954,
CC 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; KL669615; KFW76833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093PIZ7; -.
DR STRING; 328815.ENSMVIP00005024046; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016215; F:acyl-CoA desaturase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR PANTHER; PTHR11351:SF102; STEAROYL-COA DESATURASE; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU000581};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU000581};
KW Lipid metabolism {ECO:0000256|RuleBase:RU000581};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000581};
KW Reference proteome {ECO:0000313|Proteomes:UP000053258};
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 71..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..301
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW76833.1"
FT NON_TER 354
FT /evidence="ECO:0000313|EMBL:KFW76833.1"
SQ SEQUENCE 354 AA; 40363 MW; 2A5540DF94BB8F4C CRC64;
LSKEFSSTSS PTAVGTVTSR ATRNGNAIVE KNLLNHEDLA GDRGMIDDLF DETYREKEGP
KPPLRYVWRN IILMSLLHLG AIFALTLIPS AKIQTLAWGL LVLFCVALGI TAGSHRLWSH
RSYKATLPLR IFLTIANSMA FQNDIYEWVR DHRVHHKFSE TDADPHNAMR GFFFSHIGWL
LVRKHPDVIE KGQKLDLSDI KADKVVMFQR RYYKPSVVLL CFTLPTVVPW YFWDESIVIS
FFIPAILRYT IGLNATWLVN SAAHMFGNRP YDQNINPREN PLVSLGALGE GFHNYHHTFP
YDYSTSEFGW RFNLTTAFID LMCLLGLASD RKKVSKEVIL ARKMRTGDGS HKSG
//
