D5FAD_THRSP
ID D5FAD_THRSP Reviewed; 439 AA.
AC Q8S3C1;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Acyl-lipid (8-3)-desaturase;
DE EC=1.14.19.30 {ECO:0000305|PubMed:11397798};
DE AltName: Full=AN Delta(5)-fatty-acid desaturase;
DE AltName: Full=Acyl-lipid 5-desaturase;
DE AltName: Full=Delta-5 fatty acid desaturase {ECO:0000303|PubMed:11397798};
GN Name=Fad5 {ECO:0000303|PubMed:11397798};
OS Thraustochytrium sp.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Labyrinthulomycetes;
OC Thraustochytrida; Thraustochytriaceae; Thraustochytrium;
OC unclassified Thraustochytrium.
OX NCBI_TaxID=145168;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 21685 {ECO:0000312|EMBL:AAM09687.1};
RX PubMed=11397798; DOI=10.1074/jbc.m102971200;
RA Qiu X., Hong H., MacKenzie S.L.;
RT "Identification of a Delta 4 fatty acid desaturase from Thraustochytrium
RT sp. involved in the biosynthesis of docosahexanoic acid by heterologous
RT expression in Saccharomyces cerevisiae and Brassica juncea.";
RL J. Biol. Chem. 276:31561-31566(2001).
CC -!- FUNCTION: Fatty acid desaturase that introduces a cis double bond at
CC the 5-position in 20-carbon polyunsaturated fatty acids incorporated in
CC a glycerolipid that contain a Delta(8) double bond.
CC {ECO:0000269|PubMed:11397798}.
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;
CC Evidence={ECO:0000305|PubMed:11397798};
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;
CC Evidence={ECO:0000305|PubMed:11397798};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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 -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF489588; AAM09687.1; -; mRNA.
DR AlphaFoldDB; Q8S3C1; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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; IDA:UniProtKB.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.10.120.10; -; 1.
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; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR SUPFAM; SSF55856; SSF55856; 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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..439
FT /note="Acyl-lipid (8-3)-desaturase"
FT /id="PRO_0000434759"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 7..88
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 171..175
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 208..213
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 376..380
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 40
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 66
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 439 AA; 49832 MW; EBC272B29E59B73A CRC64;
MGKGSEGRSA AREMTAEANG DKRKTILIEG VLYDATNFKH PGGSIINFLT EGEAGVDATQ
AYREFHQRSG KADKYLKSLP KLDASKVESR FSAKEQARRD AMTRDYAAFR EELVAEGYFD
PSIPHMIYRV VEIVALFALS FWLMSKASPT SLVLGVVMNG IAQGRCGWVM HEMGHGSFTG
VIWLDDRMCE FFYGVGCGMS GHYWKNQHSK HHAAPNRLEH DVDLNTLPLV AFNERVVRKV
KPGSLLALWL RVQAYLFAPV SCLLIGLGWT LYLHPRYMLR TKRHMEFVWI FARYIGWFSL
MGALGYSPGT SVGMYLCSFG LGCIYIFLQF AVSHTHLPVT NPEDQLHWLE YAADHTVNIS
TKSWLVTWWM SNLNFQIEHH LFPTAPQFRF KEISPRVEAL FKRHNLPYYD LPYTSAVSTT
FANLYSVGHS VGADTKKQD
