ID A0A168R4T8_ABSGL Unreviewed; 389 AA.
AC A0A168R4T8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Fatty acid desaturase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=ABSGL_11980.1 scaffold 12361 {ECO:0000313|EMBL:SAM06104.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM06104.1};
RN [1] {ECO:0000313|EMBL:SAM06104.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM06104.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295}.
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DR EMBL; LT554490; SAM06104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168R4T8; -.
DR STRING; 4829.A0A168R4T8; -.
DR InParanoid; A0A168R4T8; -.
DR OMA; IGQHIFH; -.
DR OrthoDB; 4215at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR CDD; cd03507; Delta12-FADS-like; 1.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR021863; FAS_N.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR32100:SF35; OMEGA-3 FATTY ACID DESATURASE FAT-1; 1.
DR PANTHER; PTHR32100; OMEGA-6 FATTY ACID DESATURASE, CHLOROPLASTIC; 1.
DR Pfam; PF11960; DUF3474; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..66
FT /note="Fatty acid desaturase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11960"
FT DOMAIN 85..358
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 389 AA; 44392 MW; 6E07F279E8BC907F CRC64;
MATQRNVPTD RKEEGPIIDE AIERGWEIPD FTIKEIRDAI PAHCFRRDTF RSFTYVFHDV
AIILALGYAA TYIDHVSSLP ARIALWSLYW VAQGIVGTGV WVIGHECGHQ AFSPSKAINN
GVGMVLHSLL LVPYHSWRFS HSRHHKATGH MTKDQVFVPH TRKAVGLPAR DVDPEGDGPH
SALEESPIAM LYSMFLMFVF GWPLYLFTNV TGQPYPGWAS HFNPYCDIFD SNQVADVYKS
VLGMFVAIGG LVYAGQVFGS LAIVKYYVIP YLFVNFWLVL ITYLQHTDPT LPHYRENVWN
FQRGAALTVD RSYGFLLDYF HHHISDTHVA HHFFSTMPHY HAEEATVHIK KALGKHYKYD
PTPIPQALYK SWIGCRFVED DGDVVFFKN
//
