ID   LLCD_SYNY3              Reviewed;         359 AA.
AC   Q08871;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Acyl-CoA 6-desaturase;
DE            EC=1.14.19.3;
DE   AltName: Full=Delta(6)-desaturase;
DE   AltName: Full=Linoleoyl-CoA desaturase;
GN   Name=des6; OrderedLocusNames=sll0262;
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].
RX   PubMed=8389613; DOI=10.1007/bf00014936;
RA   Reddy A.S., Nuccio M.L., Gross L.M., Thomas T.L.;
RT   "Isolation of a delta 6-desaturase gene from the cyanobacterium
RT   Synechocystis sp. strain PCC 6803 by gain-of-function expression in
RT   Anabaena sp. strain PCC 7120.";
RL   Plant Mol. Biol. 22:293-300(1993).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC         H(+) + O2 = (6Z,9Z,12Z)-octadecatrienoyl-CoA + 2 Fe(III)-[cytochrome
CC         b5] + 2 H2O; Xref=Rhea:RHEA:47140, 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:57363,
CC         ChEBI:CHEBI:57383; EC=1.14.19.3;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] +
CC         2 H(+) + O2 = (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + 2 Fe(III)-
CC         [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:47144, Rhea:RHEA-COMP:10438,
CC         Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:71489, ChEBI:CHEBI:74034; EC=1.14.19.3;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; L11421; AAA27286.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18502.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q08871; -.
DR   SMR; Q08871; -.
DR   IntAct; Q08871; 3.
DR   STRING; 1148.1653589; -.
DR   PaxDb; Q08871; -.
DR   EnsemblBacteria; BAA18502; BAA18502; BAA18502.
DR   KEGG; syn:sll0262; -.
DR   eggNOG; COG3239; Bacteria.
DR   InParanoid; Q08871; -.
DR   OMA; HQVEHHI; -.
DR   PhylomeDB; Q08871; -.
DR   BioCyc; MetaCyc:MON-16955; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0016213; F:linoleoyl-CoA desaturase activity; IEA:UniProtKB-EC.
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   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.
PE   3: Inferred from homology;
KW   Iron; Oxidoreductase; Reference proteome.
FT   CHAIN           1..359
FT                   /note="Acyl-CoA 6-desaturase"
FT                   /id="PRO_0000185432"
SQ   SEQUENCE   359 AA;  41425 MW;  33FB165AEB98C05F CRC64;
     MLTAERIKFT QKRGFRRVLN QRVDAYFAEH GLTQRDNPSM YLKTLIIVLW LFSAWAFVLF
     APVIFPVRLL GCMVLAIALA AFSFNVGHDA NHNAYSSNPH INRVLGMTYD FVGLSSFLWR
     YRHNYLHHTY TNILGHDVEI HGDGAVRMSP EQEHVGIYRF QQFYIWGLYL FIPFYWFLYD
     VYLVLNKGKY HDHKIPPFQP LELASLLGIK LLWLGYVFGL PLALGFSIPE VLIGASVTYM
     TYGIVVCTIF MLAHVLESTE FLTPDGESGA IDDEWAICQI RTTANFATNN PFWNWFCGGL
     NHQVTHHLFP NICHIHYPQL ENIIKDVCQE FGVEYKVYPT FKAAIASNYR WLEAMGKAS