FAD5A_DICDI
ID FAD5A_DICDI Reviewed; 464 AA.
AC Q9Y1W0; Q54NI8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Delta(5) fatty acid desaturase A;
DE Short=Delta-5 fatty acid desaturase A;
DE EC=1.14.19.-;
GN Name=fadA; Synonyms=des5-1; ORFNames=DDB_G0285211;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS DESATURASE.
RC STRAIN=AX2;
RX PubMed=10504413; DOI=10.1046/j.1432-1327.1999.00789.x;
RA Saito T., Ochiai H.;
RT "Identification of Delta5-fatty acid desaturase from the cellular slime
RT mold Dictyostelium discoideum.";
RL Eur. J. Biochem. 265:809-814(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=AX2;
RX PubMed=15632431; DOI=10.1099/mic.0.27651-0;
RA Saito T., Kato A., Ochiai H., Morita N.;
RT "Temperature adaptation in Dictyostelium: role of Delta5 fatty acid
RT desaturase.";
RL Microbiology 151:113-119(2005).
CC -!- FUNCTION: Specific for desaturation of the 5 position in C16 and C18
CC fatty acids. {ECO:0000269|PubMed:10504413}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutants show a significant decrease in the amount
CC of dienoic acids with a concomitant increase in their monoenoic acid
CC precursors, and have an increased tolerance to heat shock.
CC {ECO:0000269|PubMed:15632431}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AB029311; BAA81814.1; -; Genomic_DNA.
DR EMBL; AAFI02000076; EAL64817.1; -; Genomic_DNA.
DR RefSeq; XP_638329.1; XM_633237.1.
DR AlphaFoldDB; Q9Y1W0; -.
DR SMR; Q9Y1W0; -.
DR STRING; 44689.DDB0191456; -.
DR PaxDb; Q9Y1W0; -.
DR EnsemblProtists; EAL64817; EAL64817; DDB_G0285211.
DR GeneID; 8624999; -.
DR KEGG; ddi:DDB_G0285211; -.
DR dictyBase; DDB_G0285211; fadA.
DR eggNOG; KOG4232; Eukaryota.
DR HOGENOM; CLU_030320_1_0_1; -.
DR InParanoid; Q9Y1W0; -.
DR OMA; GPFWIRE; -.
DR PhylomeDB; Q9Y1W0; -.
DR PRO; PR:Q9Y1W0; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IC:dictyBase.
DR GO; GO:0062076; F:acyl-CoA delta5-desaturase activity; IDA:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:dictyBase.
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; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:dictyBase.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IMP:dictyBase.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:dictyBase.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Electron transport; Fatty acid biosynthesis; Fatty acid metabolism; Heme;
KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..464
FT /note="Delta(5) fatty acid desaturase A"
FT /id="PRO_0000327535"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 13..90
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 176..180
FT /note="Histidine box-1"
FT MOTIF 212..217
FT /note="Histidine box-2"
FT MOTIF 396..400
FT /note="Histidine box-3"
FT BINDING 48
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 71
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
SQ SEQUENCE 464 AA; 54005 MW; E9F90BC5CB5B82E1 CRC64;
MYYSNKMSKV ITGKQYSWSE LAKHNTENDC WVAVDGKVYD ITRWVPLHPG GKEVLLLAAG
RDVTNLFESY HPMSDKPTSI LKNYEIGYIS SYEHPKFVQK SDFYKTLKER VRKHFKATDQ
DPQMAVSIFS RLALVYLLVF VTYYLAHYTS NNFYLNCFLA IVYALCNSLF SMHMMHDSCH
AAISHYPGVW KWMGASFDFV TGASFLSWCH QHVIGHHIYT NVRNADPDLG QGEVDFRIVT
PFQTRSWYHK YQHIYAPLLY GIYTLKYRTQ DWEAFVKDGK NGAIRVSVAT NFDKAAYVIG
KLSFVFFRFI LPLRYHSFTD LICYFLIAEF VFGWYLTINF QVSHVAEDLK FFATPERPDE
PSQINEDWAI LQLKTTQDYG HGSLLCTFFS GSLNHQVVHH LFPSIAQDFY PQLVPIVKEV
CKEHNITYHI KPNFTEAIMS HINYLYKMGN DPDYVKKPLA SKDD
