ID Q8F1G4_LEPIN Unreviewed; 278 AA.
AC Q8F1G4;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Aldo/keto reductase {ECO:0000313|EMBL:AAN50370.1};
GN Name=ara1 {ECO:0000313|EMBL:AAN50370.1};
GN OrderedLocusNames=LA_3172 {ECO:0000313|EMBL:AAN50370.1};
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:AAN50370.1, ECO:0000313|Proteomes:UP000001408};
RN [1] {ECO:0000313|EMBL:AAN50370.1, ECO:0000313|Proteomes:UP000001408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601 {ECO:0000313|EMBL:AAN50370.1,
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE010300; AAN50370.1; -; Genomic_DNA.
DR RefSeq; NP_713352.1; NC_004342.2.
DR RefSeq; WP_001060166.1; NC_004342.2.
DR AlphaFoldDB; Q8F1G4; -.
DR STRING; 189518.LA_3172; -.
DR PaxDb; 189518-LA_3172; -.
DR EnsemblBacteria; AAN50370; AAN50370; LA_3172.
DR GeneID; 61144276; -.
DR KEGG; lil:LA_3172; -.
DR PATRIC; fig|189518.3.peg.3151; -.
DR HOGENOM; CLU_023205_0_1_12; -.
DR InParanoid; Q8F1G4; -.
DR OrthoDB; 9804790at2; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd19071; AKR_AKR1-5-like; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43827; 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE; 1.
DR PANTHER; PTHR43827:SF3; ALDO-KETO REDUCTASE; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 2.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001408}.
FT DOMAIN 23..265
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 57
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 82
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 278 AA; 31973 MW; 0C59AB818B937ED1 CRC64;
MNNKENPLKQ TIMLNNGISM PILGLGVWKT KSGKECKEAV LNALEAGYRH IDTARIYDNE
VDVGQAIRES GIPRKEIFIT TKLWNADQGS DKTRKALENS LDRLGIDFVD LYLIHFPVTS
KRMDSWKELE KLYHDKLCKA IGVSNYTIIH LTELLKNSQI TPAVNQVEFH PFLNQIHLLE
YCKKHKIQLE AYSPLAHGQK IEDPTIAKIA QKYDKTPAQI LIRWAIEQKI VVIPKSIKKE
RIIENSKVFD FAISEEDMKI LNSLDEDFRT CWDPSEVV
//
