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Database: UniProt
Entry: A0A1T5P1K9_9BACT
LinkDB: A0A1T5P1K9_9BACT
Original site: A0A1T5P1K9_9BACT 
ID   A0A1T5P1K9_9BACT        Unreviewed;       366 AA.
AC   A0A1T5P1K9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Linoleoyl-CoA desaturase {ECO:0000313|EMBL:SKD06238.1};
GN   ORFNames=SAMN05660461_3356 {ECO:0000313|EMBL:SKD06238.1};
OS   Chitinophaga ginsengisegetis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=393003 {ECO:0000313|EMBL:SKD06238.1, ECO:0000313|Proteomes:UP000190166};
RN   [1] {ECO:0000313|EMBL:SKD06238.1, ECO:0000313|Proteomes:UP000190166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18108 {ECO:0000313|EMBL:SKD06238.1,
RC   ECO:0000313|Proteomes:UP000190166};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUZZ01000002; SKD06238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5P1K9; -.
DR   STRING; 393003.SAMN05660461_3356; -.
DR   Proteomes; UP000190166; 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   Reference proteome {ECO:0000313|Proteomes:UP000190166};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        71..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        210..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        237..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          71..345
FT                   /note="Fatty acid desaturase"
FT                   /evidence="ECO:0000259|Pfam:PF00487"
SQ   SEQUENCE   366 AA;  42345 MW;  607122FD1EDB723D CRC64;
     MKKDEWHIVR FASRGNNSFI ESAKAAVQDY FSPNNISVYA NREMWIKTIV MLSLYFVPYT
     LMVVGLGAGN VWLYLGLWLL TGLGVTGIGA SIMHDANHGS FSPKKGINDM IGHILEIIGG
     YAPTWKIQHN VLHHTYTNVT GLDEDIDSIK FLRFSPNQPR HWYHRYQHMY AWGFYMLMTL
     FWMTAKDYLQ VLRYKSHGLL SKQKVTLKQA MFRISLFKVI YYGYILVLPL IFSGMPWYWV
     LAGFFLMHFT AGLLLACIFQ PAHVMSSSGY ATPDADRKMK DSWAVHEMEN TTNYAPRSRV
     LSWCIGGLNY QIEHHLFSGI CHVHYRKLAP IVKQQAAAFN IPYQVQPTFI RALWEHARML
     KKLGRK
//
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