ID Q8EXY9_LEPIN Unreviewed; 273 AA.
AC Q8EXY9;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Fatty-acid desaturase {ECO:0000313|EMBL:AAN51627.1};
GN Name=ole1 {ECO:0000313|EMBL:AAN51627.1};
GN OrderedLocusNames=LB_068 {ECO:0000313|EMBL:AAN51627.1};
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=189518 {ECO:0000313|EMBL:AAN51627.1, ECO:0000313|Proteomes:UP000001408};
RN [1] {ECO:0000313|EMBL:AAN51627.1, ECO:0000313|Proteomes:UP000001408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601 {ECO:0000313|EMBL:AAN51627.1,
RC ECO:0000313|Proteomes:UP000001408};
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.X., Fu G., Jiang X.G., Zeng R., Miao Y.G., Xu H., Zhang Y.X.,
RA Xiong H., Lu G., Lu L.F., Jiang H.Q., Jia J., Tu Y.F., Jiang J.X., Gu W.Y.,
RA Zhang Y.Q., Cai Z., Sheng H.H., Yin H.F., Zhang Y., Zhu G.F., Wan M.,
RA Huang H.L., Qian Z., Wang S.Y., Ma W., Yao Z.J., Shen Y., Qiang B.Q.,
RA Xia Q.C., Guo X.K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.M.,
RA Shi M.H., Chen Z., Xu J.G., Zhao G.P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AE010301; AAN51627.1; -; Genomic_DNA.
DR RefSeq; NP_714612.1; NC_004343.2.
DR RefSeq; WP_000511395.1; NC_004343.2.
DR AlphaFoldDB; Q8EXY9; -.
DR STRING; 189518.LB_068; -.
DR PaxDb; 189518-LB_068; -.
DR EnsemblBacteria; AAN51627; AAN51627; LB_068.
DR GeneID; 61141529; -.
DR KEGG; lil:LB_068; -.
DR PATRIC; fig|189518.3.peg.4392; -.
DR HOGENOM; CLU_096051_0_0_12; -.
DR InParanoid; Q8EXY9; -.
DR OrthoDB; 19906at2; -.
DR Proteomes; UP000001408; Chromosome II.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd03505; Delta9-FADS-like; 1.
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.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001408};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 128..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..232
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 273 AA; 32169 MW; BA104759AC290221 CRC64;
MGIILSFFIG HWFLSAFVQS FFLHRYAAHA MFKMNKFWEK FFYIFTCVAQ GSSFLNPRAY
AIMHRQHHAY SDTGKDPHSP VASKGFLDMM WKTALNYEAI LEETTNVEKE FKGNYPEWPA
IDVLSNSWTF RLFCGTLYTL FYFYFVPEGQ YAWYLLLPIH WLMGPLHGAI VNWCGHMYGY
RNHKKNPDNS KNTLFVDFMI AGELYQNNHH AHPNSPNFAF RWFELDFTYQ VMKILHFFRI
IKIQRAVWTE KGKKILRGSE VLVEPTSTST VAA
//
