FAD5B_DICDI
ID FAD5B_DICDI Reviewed; 467 AA.
AC O96099; Q54SX8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Acyl-lipid (8-3)-desaturase B;
DE EC=1.14.19.30 {ECO:0000305};
DE AltName: Full=Delta(5) fatty acid desaturase B {ECO:0000303|PubMed:10712614};
DE Short=Delta-5 fatty acid desaturase B {ECO:0000303|PubMed:10712614};
GN Name=fadB; Synonyms=des5-2; ORFNames=DDB_G0282147;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION AS DESATURASE.
RC STRAIN=AX2;
RX PubMed=10712614; DOI=10.1046/j.1432-1327.2000.01180.x;
RA Saito T., Morio T., Ochiai H.;
RT "A second functional Delta5 fatty acid desaturase in the cellular slime
RT mould Dictyostelium discoideum.";
RL Eur. J. Biochem. 267:1813-1818(2000).
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).
RN [4]
RP IDENTIFICATION.
RX PubMed=17291553; DOI=10.1016/j.phytochem.2006.12.016;
RA Zhou X.R., Robert S.S., Petrie J.R., Frampton D.M., Mansour M.P.,
RA Blackburn S.I., Nichols P.D., Green A.G., Singh S.P.;
RT "Isolation and characterization of genes from the marine microalga Pavlova
RT salina encoding three front-end desaturases involved in docosahexaenoic
RT acid biosynthesis.";
RL Phytochemistry 68:785-796(2007).
CC -!- FUNCTION: Fatty acid desaturase that introduces a cis double bond at
CC the 5-position in 18-carbon polyunsaturated fatty acids.
CC {ECO:0000269|PubMed:10712614}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (8Z,11Z,14Z)-icosatrienoyl-containing glycerolipid + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5]
CC + 2 H2O; Xref=Rhea:RHEA:46260, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:90076,
CC ChEBI:CHEBI:90077; EC=1.14.19.30; Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (8Z,11Z,14Z,17Z)-eicosatetraenoyl-containing glycerolipid +
CC 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5]
CC + 2 H2O; Xref=Rhea:RHEA:46264, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:90082,
CC ChEBI:CHEBI:90083; EC=1.14.19.30; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain acts as the direct
CC electron donor to the active site of the desaturase, and does not
CC require an external cytochrome. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutants show no significant alteration in fatty
CC acid composition or in phenotype. {ECO:0000269|PubMed:15632431}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AB022097; BAA37090.1; -; mRNA.
DR EMBL; AAFI02000045; EAL66353.1; -; Genomic_DNA.
DR RefSeq; XP_640331.1; XM_635239.1.
DR AlphaFoldDB; O96099; -.
DR SMR; O96099; -.
DR STRING; 44689.DDB0214992; -.
DR PaxDb; O96099; -.
DR EnsemblProtists; EAL66353; EAL66353; DDB_G0282147.
DR GeneID; 8623432; -.
DR KEGG; ddi:DDB_G0282147; -.
DR dictyBase; DDB_G0282147; fadB.
DR eggNOG; KOG4232; Eukaryota.
DR HOGENOM; CLU_030320_1_0_1; -.
DR InParanoid; O96099; -.
DR OMA; MRTTANF; -.
DR PhylomeDB; O96099; -.
DR PRO; PR:O96099; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IC:dictyBase.
DR GO; GO:0102866; F:di-homo-gamma-linolenate delta5 desaturase activity; IEA:RHEA.
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:0006629; P:lipid metabolic process; IBA:GO_Central.
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..467
FT /note="Acyl-lipid (8-3)-desaturase B"
FT /id="PRO_0000327536"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 12..89
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 175..179
FT /note="Histidine box-1"
FT MOTIF 211..216
FT /note="Histidine box-2"
FT MOTIF 400..404
FT /note="Histidine box-3"
FT BINDING 47
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 70
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 467 AA; 54463 MW; 394F3AC7D4CB5B78 CRC64;
MMETNNENKE KLKLYTWDEV SKHNQKNDLW IIVDGKVYNI TKWVPLHPGG EDILLLSAGR
DATNLFESYH PMTDKHYSLI KQYEIGYISS YEHPKYVEKS EFYSTLKQRV RKHFQTSSQD
PKVSVGVFTR MVLIYLFLFV TYYLSQFSTD RFWLNCIFAV LYGVANSLFG LHTMHDACHT
AITHNPMTWK ILGATFDLFA GASFYAWCHQ HVIGHHLYTN VRNADPDLGQ GEIDFRVVTP
YQARSWYHKY QHIYAPILYG VYALKYRIQD HEIFTKKSNG AIRYSPISTI DTAIFILGKL
VFIISRFILP LIYNHSFSHL ICFFLISELV LGWYLAISFQ VSHVVEDLQF MATPEIFDGA
DHPLPTTFNQ DWAILQVKTT QDYAQDSVLS TFFSGGLNLQ VIHHCFPTIA QDYYPQIVPI
LKEVCKEYNV TYHYKPTFTE AIKSHINYLY KMGNDPDYVR KPVNKND
