ID Q5TM04_PSEF5 Unreviewed; 328 AA.
AC Q5TM04;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=2-ketogalactonate reductase {ECO:0000313|EMBL:BAD69623.1};
DE SubName: Full=Glyoxylate/hydroxypyruvate reductase B {ECO:0000313|EMBL:AAY91990.1};
DE EC=1.1.1.79 {ECO:0000313|EMBL:AAY91990.1};
GN Name=2-KGalARE {ECO:0000313|EMBL:BAD69623.1};
GN Synonyms=ghrB1 {ECO:0000313|EMBL:AAY91990.1};
GN OrderedLocusNames=PFL_2717 {ECO:0000313|EMBL:AAY91990.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:BAD69623.1};
RN [1] {ECO:0000313|EMBL:BAD69623.1}
RP NUCLEOTIDE SEQUENCE.
RA Tanimura R., Nomoto R., Hosaka H., Matsuura T., Nakagawa A., Ikehara K.,
RA Iwamoto R.;
RT "Purification and characterization of a noble 2-keto-D-galactonic acid
RT reductase from P. fluorescens.";
RL Seikagaku 76:792-792(2004).
RN [2] {ECO:0000313|EMBL:AAY91990.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540}, and Pf-5
RC {ECO:0000313|EMBL:AAY91990.1};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
RN [3] {ECO:0000313|EMBL:AAY91990.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Pf-5 {ECO:0000313|EMBL:AAY91990.1};
RA Loper J.E., Davis E.W., Hartney S.L., Shaffer B.T., Hassan K.A.,
RA Brinkac L.M., Durkin A., Paulsen I.T.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP000076; AAY91990.1; -; Genomic_DNA.
DR EMBL; AB162195; BAD69623.1; -; Genomic_DNA.
DR RefSeq; WP_011061011.1; NC_004129.6.
DR AlphaFoldDB; Q5TM04; -.
DR STRING; 220664.PFL_2717; -.
DR KEGG; pfl:PFL_2717; -.
DR PATRIC; fig|220664.5.peg.2771; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_6; -.
DR BioCyc; MetaCyc:MONOMER-12749; -.
DR Proteomes; UP000008540; Chromosome.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) 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; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:AAY91990.1}; Pyruvate {ECO:0000313|EMBL:AAY91990.1}.
FT DOMAIN 6..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 35885 MW; 525A2E97FCDFE079 CRC64;
MKKHLVLYKK LSPTLMARLQ EQAQVTLIET LDAAGLNALR QALPSADGLL GASLRLDAEL
LDLAPRLRAV ASVSVGVDNY DIDYLTQRRI LLSNTPDVLT ETTADTGFAL ILATARRVVE
LANLVRAGQW QRNIGPAHFG TDVHGKTLGI IGMGRIGEAL AQRGHFGFGM PLIYHSTRPK
PAVEQRFNAQ YRSLEQLLEE ADFICLTLPL TERTQGLIGA REFALMRPES IFINISRGKV
VDEAALIEAL QQRRIRGAGL DVFEREPLDH DSPLLQLPNV VATPHIGSAT HETREAMARC
AVDNLLAALA GQRPPNLVNP AAWTSPRP
//
