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Database: UniProt
Entry: Q88NF1_PSEPK
LinkDB: Q88NF1_PSEPK
Original site: Q88NF1_PSEPK 
ID   Q88NF1_PSEPK            Unreviewed;       324 AA.
AC   Q88NF1;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   SubName: Full=2-ketoaldonate reductase / hydroxypyruvate/glyoxylate reductase {ECO:0000313|EMBL:AAN66885.1};
DE            EC=1.1.1.215 {ECO:0000313|EMBL:AAN66885.1};
DE            EC=1.1.1.79 {ECO:0000313|EMBL:AAN66885.1};
DE            EC=1.1.1.81 {ECO:0000313|EMBL:AAN66885.1};
GN   Name=ghrB {ECO:0000313|EMBL:AAN66885.1};
GN   OrderedLocusNames=PP_1261 {ECO:0000313|EMBL:AAN66885.1};
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN66885.1, ECO:0000313|Proteomes:UP000000556};
RN   [1] {ECO:0000313|EMBL:AAN66885.1, ECO:0000313|Proteomes:UP000000556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC   {ECO:0000313|Proteomes:UP000000556};
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., Madupu R.,
RA   Nelson W., White O., Peterson J., Khouri H., Hance I., Chris Lee P.,
RA   Holtzapple E., Scanlan D., Tran K., Moazzez A., Utterback T., Rizzo M.,
RA   Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D.,
RA   Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N.,
RA   Dusterhoft A., Tummler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; AE015451; AAN66885.1; -; Genomic_DNA.
DR   RefSeq; NP_743421.1; NC_002947.4.
DR   RefSeq; WP_010952394.1; NC_002947.4.
DR   AlphaFoldDB; Q88NF1; -.
DR   STRING; 160488.PP_1261; -.
DR   PaxDb; 160488-PP_1261; -.
DR   GeneID; 83682305; -.
DR   KEGG; ppu:PP_1261; -.
DR   PATRIC; fig|160488.4.peg.1337; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_2_6; -.
DR   OrthoDB; 9805416at2; -.
DR   PhylomeDB; Q88NF1; -.
DR   BioCyc; PPUT160488:G1G01-1348-MONOMER; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0008873; F:gluconate 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd05301; GDH; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000556}.
FT   DOMAIN          5..318
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          108..286
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   324 AA;  34919 MW;  59440106AEF22C8D CRC64;
     MKKTVLAFSR ITPAMAERLQ QDFNVILPNP KLGDISAQFN EALPEAHGLI GVGRKLGRAQ
     LEGAARLEVV SSVSVGYDNY DLDYFNERGI ALTNTPDVLT ESTADLGFSL IMGCARRTAE
     LDAWTKAGNW QATVGPAHFG SDVHGKTLGI VGMGNIGAAV ARRGRFGFNM PILYSGNSRK
     TALEKELGAQ FRSLDQLLAE ADFVVIVVPL SDATRKLISS RELKLMKPSA FLINIARGPV
     VDEAALIEAL QAGTIRGTGL DVYEKEPLSD SPLFKLPNAL TLPHIGSATA ETREAMANRA
     IDNLRAALLG ERPRDLVNPQ VWKG
//
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