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Database: UniProt
Entry: A0A0C1H6D8_9BACT
LinkDB: A0A0C1H6D8_9BACT
Original site: A0A0C1H6D8_9BACT 
ID   A0A0C1H6D8_9BACT        Unreviewed;       382 AA.
AC   A0A0C1H6D8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Putative acyl-CoA desaturase {ECO:0000313|EMBL:KIC73039.1};
DE            EC=1.14.19.1 {ECO:0000313|EMBL:KIC73039.1};
GN   ORFNames=DB42_CK00080 {ECO:0000313|EMBL:KIC73039.1};
OS   Neochlamydia sp. EPS4.
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC   Neochlamydia.
OX   NCBI_TaxID=1478175 {ECO:0000313|EMBL:KIC73039.1, ECO:0000313|Proteomes:UP000031344};
RN   [1] {ECO:0000313|EMBL:KIC73039.1, ECO:0000313|Proteomes:UP000031344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS4 {ECO:0000313|EMBL:KIC73039.1,
RC   ECO:0000313|Proteomes:UP000031344};
RX   PubMed=25069652; DOI=10.1093/molbev/msu227;
RA   Domman D., Collingro A., Lagkouvardos I., Gehre L., Weinmaier T.,
RA   Rattei T., Subtil A., Horn M.;
RT   "Massive expansion of Ubiquitination-related gene families within the
RT   Chlamydiae.";
RL   Mol. Biol. Evol. 31:2890-2904(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIC73039.1}.
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DR   EMBL; JSDQ01000083; KIC73039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1H6D8; -.
DR   STRING; 1478175.DB42_CK00080; -.
DR   PATRIC; fig|1478175.3.peg.1842; -.
DR   Proteomes; UP000031344; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd03505; Delta9-FADS-like; 1.
DR   InterPro; IPR009160; Acyl-CoA_deSatase_haem/ster-bd.
DR   InterPro; IPR015876; Acyl-CoA_DS.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR   PANTHER; PTHR11351:SF31; DESATURASE 1, ISOFORM A-RELATED; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   PIRSF; PIRSF000345; OLE1; 1.
DR   PRINTS; PR00075; FACDDSATRASE.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KIC73039.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        47..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..276
FT                   /note="Fatty acid desaturase"
FT                   /evidence="ECO:0000259|Pfam:PF00487"
SQ   SEQUENCE   382 AA;  45526 MW;  006DEFCE827396B9 CRC64;
     MLYNLWLSMI NLKKGVNWSP TIFLIIFQVA LIIWLPFYFY YNRPTLSMVA ASVVLLYATG
     LSITGGYHRF YSHRSYKTNL FLEWLLLFFG SMAGQGSALR WSYDHRLHHA FVDTDKDPYS
     IQKGFWYAHF LWIIEKPRPI NPKVVSDLIS NPLVVFQHRF YVFLFILTNS LVFLSLGWFL
     NDYIGALTFA VGVRLFCLYH STWFINSLAH TWGDQPFSQE HSAVNNYIIS FLTFGEGYHN
     YHHTYANDYR NGIYWYQFDP TKWLIWLLSK LGLAYHLRTT DKYTIKKRMV TEHAYLLQEK
     LVKSWESKRI EWEPIINELA SSLVRKMTDF SQLKSRYREL KTQCTEAPLL KEIKKEMKAL
     QKSLRQDWKK WWQLSKTIMS HA
//
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