DESA_SYNY3
ID DESA_SYNY3 Reviewed; 351 AA.
AC P20388;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Delta(12)-fatty-acid desaturase;
DE EC=1.14.19.6 {ECO:0000269|PubMed:2118597};
GN Name=desA; OrderedLocusNames=slr1350;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2118597; DOI=10.1038/347200a0;
RA Wada H., Gombos Z., Murata N.;
RT "Enhancement of chilling tolerance of a cyanobacterium by genetic
RT manipulation of fatty acid desaturation.";
RL Nature 347:200-203(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Can introduce a second cis double bond at the Delta(12)
CC position of fatty acid bound to membranes glycerolipids. This enzyme is
CC involved in chilling tolerance because the phase transition temperature
CC of lipids of cellular membranes depends on the degree of unsaturation
CC of fatty acids of the membrane lipids. {ECO:0000269|PubMed:2118597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:25856, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:57387; EC=1.14.19.6;
CC Evidence={ECO:0000269|PubMed:2118597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = (9Z,12Z)-hexadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:45096, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:61540,
CC ChEBI:CHEBI:76552; EC=1.14.19.6;
CC Evidence={ECO:0000269|PubMed:2118597};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; X53508; CAA37584.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18169.1; -; Genomic_DNA.
DR PIR; S11519; S11519.
DR AlphaFoldDB; P20388; -.
DR IntAct; P20388; 3.
DR STRING; 1148.1653254; -.
DR PaxDb; P20388; -.
DR EnsemblBacteria; BAA18169; BAA18169; BAA18169.
DR KEGG; syn:slr1350; -.
DR eggNOG; COG3239; Bacteria.
DR InParanoid; P20388; -.
DR OMA; CGHRSFA; -.
DR PhylomeDB; P20388; -.
DR BioCyc; MetaCyc:MON-16956; -.
DR BRENDA; 1.14.19.45; 382.
DR BRENDA; 1.14.19.6; 382.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102985; F:delta12-fatty-acid desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102987; F:palmitoleic acid delta 12 desaturase activity; IEA:RHEA.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR005803; FADS-2_CS.
DR Pfam; PF00487; FA_desaturase; 1.
DR PROSITE; PS00574; FATTY_ACID_DESATUR_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="Delta(12)-fatty-acid desaturase"
FT /id="PRO_0000185417"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 90..94
FT /note="Histidine box-1"
FT MOTIF 126..130
FT /note="Histidine box-2"
FT MOTIF 287..291
FT /note="Histidine box-3"
SQ SEQUENCE 351 AA; 40495 MW; 85DBEEE341F73F77 CRC64;
MTATIPPLTP TVTPSNPDRP IADLKLQDII KTLPKECFEK KASKAWASVL ITLGAIAVGY
LGIIYLPWYC LPITWIWTGT ALTGAFVVGH DCGHRSFAKK RWVNDLVGHI AFAPLIYPFH
SWRLLHDHHH LHTNKIEVDN AWDPWSVEAF QASPAIVRLF YRAIRGPFWW TGSIFHWSLM
HFKLSNFAQR DRNKVKLSIA VVFLFAAIAF PALIITTGVW GFVKFWLMPW LVYHFWMSTF
TIVHHTIPEI RFRPAADWSA AEAQLNGTVH CDYPRWVEVL CHDINVHIPH HLSVAIPSYN
LRLAHGSLKE NWGPFLYERT FNWQLMQQIS GQCHLYDPEH GYRTFGSLKK V
