ID A5DK39_PICGU Unreviewed; 417 AA.
AC A5DK39;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Fatty acid desaturase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PGUG_03640 {ECO:0000313|EMBL:EDK39542.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK39542.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK39542.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408158; EDK39542.2; -; Genomic_DNA.
DR RefSeq; XP_001484259.1; XM_001484209.1.
DR AlphaFoldDB; A5DK39; -.
DR GeneID; 5125864; -.
DR KEGG; pgu:PGUG_03640; -.
DR VEuPathDB; FungiDB:PGUG_03640; -.
DR eggNOG; ENOG502QQNB; Eukaryota.
DR HOGENOM; CLU_033094_0_0_1; -.
DR InParanoid; A5DK39; -.
DR OMA; AHCNERS; -.
DR OrthoDB; 4215at2759; -.
DR Proteomes; UP000001997; 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 Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 106..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..80
FT /note="Fatty acid desaturase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11960"
FT DOMAIN 113..381
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 417 AA; 47834 MW; FAFCC61FF25D871A CRC64;
MSVVVEDAVS SSVSVHESKP LSGVRTPSQN LVAVDGYGKK FEVPDYTMKD ILSAIPKHCY
ERSLVKSMGY VVRDIVSMCA IGYVGHKVIP MVQIANHDTL SMVVRGGLWS LQSYLIGLFG
FGLWILAHEC GHGAFSDFQN VNDFIGWVLH SYLMVPYFSW KYSHSKHHKA TGHLTRDMVF
VPYTKDEFAE KHGVSNVAEI MEESPIWTLS VLIFQQLGGL QTYLATNATG QPYPGLSWLA
KSHYAPSSPV FDPHQYWFIV LSDIGILTTL TVVYQWYKNF GAFNMFVNWF MPWLWVNHWL
VFVTFLQHTD PSMPHYKDTE WTFARGAAAT IDRNFGFVGQ HIFHDIIETH VLHHYVSRIP
FYNAREATDA IKKVMGSHYR YEGESMWYSL WKVMRMCQYV DDDNVNGVMM FRNVNGL
//
