FAD5C_DICDI
ID FAD5C_DICDI Reviewed; 459 AA.
AC Q1ZXQ5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Probable Delta(5) fatty acid desaturase C;
DE Short=Delta-5 fatty acid desaturase C;
DE EC=1.14.19.-;
GN ORFNames=DDB_G0294553;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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).
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 -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000005; EAS66933.1; -; Genomic_DNA.
DR RefSeq; XP_001134469.1; XM_001134469.1.
DR AlphaFoldDB; Q1ZXQ5; -.
DR SMR; Q1ZXQ5; -.
DR STRING; 44689.DDB0231853; -.
DR PaxDb; Q1ZXQ5; -.
DR EnsemblProtists; EAS66933; EAS66933; DDB_G0294553.
DR GeneID; 8616927; -.
DR KEGG; ddi:DDB_G0294553; -.
DR dictyBase; DDB_G0294553; -.
DR eggNOG; KOG4232; Eukaryota.
DR HOGENOM; CLU_030320_1_0_1; -.
DR InParanoid; Q1ZXQ5; -.
DR OMA; EDWAIHQ; -.
DR PhylomeDB; Q1ZXQ5; -.
DR PRO; PR:Q1ZXQ5; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; 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; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
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; IPR018506; Cyt_B5_heme-BS.
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; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
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..459
FT /note="Probable Delta(5) fatty acid desaturase C"
FT /id="PRO_0000327537"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 9..87
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 174..178
FT /note="Histidine box-1"
FT MOTIF 210..215
FT /note="Histidine box-2"
FT MOTIF 394..398
FT /note="Histidine box-3"
FT BINDING 45
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 68
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 459 AA; 53864 MW; FCF766B733B98A66 CRC64;
MENEKKLFKK LYSWKEISKH NTIENGIWIS IDGLVYDITK FIKHHPGGEQ VLILAAGRDV
TNLFESYHPM TDLPSKMLKQ YEIGQVSTME FPKYVEKSKF YSTLKERVRE HFKKSNKDPK
FAFGIIARLI FVYWFLITSY YVSHYAFIEN FYLNCLLAIV YSLSNSLFSL HMMHDACHSA
ISHNPKVWKW LGATYDLFIG ASFFYWCNQH VIGHHVYTNI RNADPDIGDS EVDFRIVTPY
QNKYWIYKYQ HIYAPFLYGL YSIKYRLCDY SVFTEGSIGR VRTANASNFE IISFIIGKLV
FIVFRFIIPL QYHSLVNLLT YFFIAEFFFG LYLSFGFQVS HSADNLKIVA TSVNENDEPT
NVDEDWAIHQ IKTTQDYGIN SYMCLFFSGG VNLQVVHHLF PSISQEYYGE LVPIIKKVCD
EYDVHYNIQP TFYAAFKSHI DFLYNMGNNE NYVRKSVTD
