ID A0A099ZK45_TINGU Unreviewed; 322 AA.
AC A0A099ZK45;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=N309_00813 {ECO:0000313|EMBL:KGL81175.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL81175.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL81175.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL81175.1};
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; KL893790; KGL81175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099ZK45; -.
DR STRING; 94827.A0A099ZK45; -.
DR Proteomes; UP000053641; 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:UP000053641};
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 39..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..269
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL81175.1"
FT NON_TER 322
FT /evidence="ECO:0000313|EMBL:KGL81175.1"
SQ SEQUENCE 322 AA; 37019 MW; FB57AA097BDCA7C2 CRC64;
VLNQEDLAGD QSSVDDTFDD TYHEKEGPKP PLQYVWRNII LMSLLHLGGI FGLILVPYAK
IQTLAWAVVV FVVNALGITA GAHRLWSHRT YKATLPLRIF LTIANSVAFQ NDIYEWVRDH
RVHHKFSETD ADPHNAKRGF FFSHVGWLLV RKHPDVIEKG QKIDLSDVRA DKVVMFQRRY
YKPSVVLLCF MMPAVVPWYF WDESITISFF IPSILRYVIG LNAAWLVNSA AHMFGNRPYD
KNINPRENSL VSLGALGEGF HNYHHTFPYD YSASEFGWHF NLTTVFIDLM CFLGLASDRK
RVSKEVILAR KMRTGEGRQK SG
//
