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Database: UniProt
Entry: A0A1H6SNQ5_9BACT
LinkDB: A0A1H6SNQ5_9BACT
Original site: A0A1H6SNQ5_9BACT 
ID   A0A1H6SNQ5_9BACT        Unreviewed;       360 AA.
AC   A0A1H6SNQ5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Linoleoyl-CoA desaturase {ECO:0000313|EMBL:SEI65222.1};
GN   ORFNames=SAMN05216327_10362 {ECO:0000313|EMBL:SEI65222.1};
OS   Dyadobacter sp. SG02.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=1855291 {ECO:0000313|EMBL:SEI65222.1, ECO:0000313|Proteomes:UP000199631};
RN   [1] {ECO:0000313|EMBL:SEI65222.1, ECO:0000313|Proteomes:UP000199631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG02 {ECO:0000313|EMBL:SEI65222.1,
RC   ECO:0000313|Proteomes:UP000199631};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00009295}.
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DR   EMBL; FNYL01000003; SEI65222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6SNQ5; -.
DR   STRING; 1855291.SAMN05216327_10362; -.
DR   OrthoDB; 104711at2; -.
DR   Proteomes; UP000199631; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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; IEA:UniProt.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProt.
DR   CDD; cd03506; Delta6-FADS-like; 1.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR012171; Fatty_acid_desaturase.
DR   PANTHER; PTHR19353:SF19; DELTA(5) FATTY ACID DESATURASE C-RELATED; 1.
DR   PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   PIRSF; PIRSF015921; FA_sphinglp_des; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        41..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        232..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          68..339
FT                   /note="Fatty acid desaturase"
FT                   /evidence="ECO:0000259|Pfam:PF00487"
SQ   SEQUENCE   360 AA;  40939 MW;  C111AF679872301E CRC64;
     MQYQKVKFTN LEKSTFFPTL RHRVDQYFST NDICKSGGSG IIYKALFMLS LYLVPYILIL
     SNQFGMLAMA GFAFVMGLGV AGVGMSVMHD AIHGSLATSN LLNKVFGASI YLLGGNAYNW
     EVQHNRLHHT YTNIHDVDED ITGKFLLRLS FQEKQRYIHR FQHIYAFFLY SLMTLSFLWK
     DFKEISLFNE MSKSGMTKPF PKKELIRLIL TKLAYVVFIC VIPLAFTSIT FGQWLIGFMI
     MHGTAGMILS TVFQMAHVVE GAEQPEPDQT GSIENAWAVH QLQTTSNFAG KNRMLSWFIG
     GLDYQIEHHL FPTISHVHYH ALSPIVKATA LEFGLVYNAK SNFRNALGSH VRMLKNMGTR
//
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