ID I4N1X7_9PSED Unreviewed; 267 AA.
AC I4N1X7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=2,5-diketo-D-gluconate reductase B {ECO:0000313|EMBL:EIK95467.1};
DE EC=1.1.1.274 {ECO:0000313|EMBL:EIK95467.1};
GN Name=dkgB {ECO:0000313|EMBL:EIK95467.1};
GN ORFNames=PMM47T1_16800 {ECO:0000313|EMBL:EIK95467.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK95467.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK95467.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK95467.1,
RC ECO:0000313|Proteomes:UP000004339};
RX PubMed=22887683; DOI=10.1128/JB.01116-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL J. Bacteriol. 194:4789-4790(2012).
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:EIK95467.1}.
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; AJWX01000015; EIK95467.1; -; Genomic_DNA.
DR RefSeq; WP_008370950.1; NZ_AJWX01000015.1.
DR AlphaFoldDB; I4N1X7; -.
DR STRING; 1179778.PMM47T1_16800; -.
DR PATRIC; fig|1179778.3.peg.3361; -.
DR eggNOG; COG0656; Bacteria.
DR OrthoDB; 9804790at2; -.
DR Proteomes; UP000004339; Unassembled WGS sequence.
DR GO; GO:0050580; F:2,5-didehydrogluconate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd19139; AKR_AKR3F2; 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; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:EIK95467.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004339}.
FT DOMAIN 8..251
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 39
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 64
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 267 AA; 28849 MW; FEE4DCA599E307E0 CRC64;
MSIPAFGLGT FRLKDQVVID AVRTALELGY RVIDTAQIYG NEAEIGQAIA ESGVPRSELF
ITTKIWVDHF AADKLIPSLR DSLVKLRTDH VDLTLIHWPS PKGAVAVSEF MGALAEAKAL
GLTRQIGVSN FTRDLMQQAI DVVGAGEIAT NQVELHPYLQ NRAVAAFAST HGIQVTSYMT
LAYGKVINDP VIARIAERHQ ATTAQVTLAW AMQLGYAVIP SSTRRANLAS NLKATSLRLS
DADMADIAAL DRGERLTSPA SIAPVWD
//
