D4FAD_REBSA
ID D4FAD_REBSA Reviewed; 447 AA.
AC A0PJ29;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Acyl-lipid (7-3)-desaturase {ECO:0000305};
DE EC=1.14.19.31 {ECO:0000305|PubMed:17291553};
DE AltName: Full=Acyl-lipid 4-desaturase {ECO:0000305};
DE AltName: Full=Delta-4 desaturase {ECO:0000303|PubMed:17291553};
DE Short=PsD4Des {ECO:0000303|PubMed:17291553};
GN Name=D4Des {ECO:0000303|PubMed:17291553};
OS Rebecca salina (Marine microalga) (Pavlova salina).
OC Eukaryota; Haptista; Haptophyta; Pavlovales; Pavlovaceae; Rebecca.
OX NCBI_TaxID=561169;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=CS-49 {ECO:0000312|EMBL:AAY15136.1};
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 4-position in 22-carbon polyunsaturated fatty acids that contain a
CC Delta(7) double bond, resulting in the production of delta-4
CC desaturated fatty acid docosahexanoic acid (DHA).
CC {ECO:0000269|PubMed:17291553}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-containing
CC glycerolipid + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a
CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-containing glycerolipid + 2
CC Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46252, Rhea:RHEA-
CC COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:88266, ChEBI:CHEBI:88267;
CC EC=1.14.19.31; Evidence={ECO:0000305|PubMed:17291553};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (7Z,10Z,13Z,16Z)-docosatetraenoyl-containing glycerolipid +
CC 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (4Z,7Z,10Z,13Z,16Z)-
CC docosapentaenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5]
CC + 2 H2O; Xref=Rhea:RHEA:46256, 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:88264,
CC ChEBI:CHEBI:88265; EC=1.14.19.31;
CC Evidence={ECO:0000305|PubMed:17291553};
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; AY926606; AAY15136.1; -; mRNA.
DR AlphaFoldDB; A0PJ29; -.
DR SMR; A0PJ29; -.
DR PRIDE; A0PJ29; -.
DR BioCyc; MetaCyc:MON-19039; -.
DR BRENDA; 1.14.19.31; 14018.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..447
FT /note="Acyl-lipid (7-3)-desaturase"
FT /id="PRO_0000434757"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 36..94
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 173..177
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 208..213
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 386..390
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 53
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 76
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 447 AA; 49307 MW; BA08E8D9B47D6761 CRC64;
MPPSAAKQMG ASTGVHAGVT DSSAFTRKDV ADRPDLTIVG DSVYDAKAFR SEHPGGAHFV
SLFGGRDATE AFMEYHRRAW PKSRMSRFHV GSLASTEEPV AADEGYLQLC ARIAKMVPSV
SSGFAPASYW VKAGLILGSA IALEAYMLYA GKRLLPSIVL GWLFALIGLN IQHDANHGAL
SKSASVNLAL GLCQDWIGGS MILWLQEHVV MHHLHTNDVD KDPDQKAHGA LRLKPTDAWS
PMHWLQHLYL LPGETMYAFK LLFLDISELV MWRWEGEPIS KLAGYLFMPS LLLKLTFWAR
FVALPLYLAP SVHTAVCIAA TVMTGSFYLA FFFFISHNFE GVASVGPDGS ITSMTRGASF
LKRQAETSSN VGGPLLATLN GGLNYQIEHH LFPRVHHGFY PRLAPLVKAE LEARGIEYKH
YPTIWSNLAS TLRHMYALGR RPRSKAE
