D5FAD_REBSA
ID D5FAD_REBSA Reviewed; 425 AA.
AC A4KDP0;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Acyl-lipid (8-3)-desaturase;
DE EC=1.14.19.30 {ECO:0000305|PubMed:17291553};
DE AltName: Full=AN Delta(5)-fatty-acid desaturase {ECO:0000305};
DE AltName: Full=Acyl-lipid 5-desaturase {ECO:0000305};
DE AltName: Full=Delta-5 desaturase {ECO:0000303|PubMed:17291553};
GN Name=D5Des {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:ABL96295.1};
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 5-position in 20-carbon polyunsaturated fatty acids incorporated in
CC a glycerolipid that contain a Delta(8) double bond.
CC {ECO:0000269|PubMed:17291553}.
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:17291553};
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: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; DQ995517; ABL96295.1; -; mRNA.
DR AlphaFoldDB; A4KDP0; -.
DR SMR; A4KDP0; -.
DR BioCyc; MetaCyc:MON-16957; -.
DR BRENDA; 1.14.19.30; 14018.
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: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; 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; 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 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 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..425
FT /note="Acyl-lipid (8-3)-desaturase"
FT /id="PRO_0000434760"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 18..93
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..168
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 201..206
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 365..369
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
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 69
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 425 AA; 48215 MW; 522F503413D83633 CRC64;
MPPRDSYSYA APPSAQLHEV DTPQEHDKKE LVIGDRAYDV TNFVKRHPGG KIIAYQVGTD
ATDAYKQFHV RSAKADKMLK SLPSRPVHKG YSPRRADLIA DFQEFTKQLE AEGMFEPSLP
HVAYRLAEVI AMHVAGAALI WHGYTFAGIA MLGVVQGRCG WLMHEGGHYS LTGNIAFDRA
IQVACYGLGC GMSGAWWRNQ HNKHHATPQK LQHDVDLDTL PLVAFHERIA AKVKSPAMKA
WLSMQAKLFA PVTTLLVALG WQLYLHPRHM LRTKHYDELA MLGIRYGLVG YLAANYGAGY
VLACYLLYVQ LGAMYIFCNF AVSHTHLPVV EPNEHATWVE YAANHTTNCS PSWWCDWWMS
YLNYQIEHHL YPSMPQFRHP KIAPRVKQLF EKHGLHYDVR GYFEAMADTF ANLDNVAHAP
EKKMQ
