ID   GLXR_ECOLI              Reviewed;         292 AA.
AC   P77161; Q2MBR9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=2-hydroxy-3-oxopropionate reductase;
DE            EC=1.1.1.60;
DE   AltName: Full=Tartronate semialdehyde reductase;
DE            Short=TSAR;
GN   Name=glxR; Synonyms=glxB1, ybbQ; OrderedLocusNames=b0509, JW0497;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=K12 / ECL1;
RX   PubMed=10601204; DOI=10.1128/jb.181.24.7479-7484.1999;
RA   Cusa E., Obradors N., Baldoma L., Badia J., Aguilar J.;
RT   "Genetic analysis of a chromosomal region containing genes required for
RT   assimilation of allantoin nitrogen and linked glyoxylate metabolism in
RT   Escherichia coli.";
RL   J. Bacteriol. 181:7479-7484(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NADP(+) = 2-hydroxy-3-oxopropanoate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18841, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57978, ChEBI:CHEBI:58349; EC=1.1.1.60;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NAD(+) = 2-hydroxy-3-oxopropanoate + H(+) +
CC         NADH; Xref=Rhea:RHEA:18845, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57978; EC=1.1.1.60;
CC   -!- PATHWAY: Organic acid metabolism; glycolate degradation; 3-phospho-D-
CC       glycerate from glycolate: step 3/4.
CC   -!- INDUCTION: By glyoxylate.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. {ECO:0000305}.
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DR   EMBL; U89279; AAB93851.1; -; Genomic_DNA.
DR   EMBL; U82664; AAB40262.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73611.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76287.1; -; Genomic_DNA.
DR   PIR; D64782; D64782.
DR   RefSeq; NP_415042.1; NC_000913.3.
DR   RefSeq; WP_000765839.1; NZ_STEB01000007.1.
DR   AlphaFoldDB; P77161; -.
DR   SMR; P77161; -.
DR   BioGRID; 4262821; 16.
DR   BioGRID; 849534; 4.
DR   IntAct; P77161; 9.
DR   STRING; 511145.b0509; -.
DR   PaxDb; P77161; -.
DR   PRIDE; P77161; -.
DR   EnsemblBacteria; AAC73611; AAC73611; b0509.
DR   EnsemblBacteria; BAE76287; BAE76287; BAE76287.
DR   GeneID; 66671195; -.
DR   GeneID; 945146; -.
DR   KEGG; ecj:JW0497; -.
DR   KEGG; eco:b0509; -.
DR   PATRIC; fig|1411691.4.peg.1768; -.
DR   EchoBASE; EB3052; -.
DR   eggNOG; COG2084; Bacteria.
DR   HOGENOM; CLU_035117_1_0_6; -.
DR   InParanoid; P77161; -.
DR   OMA; METPYPK; -.
DR   PhylomeDB; P77161; -.
DR   BioCyc; EcoCyc:G6278-MON; -.
DR   BioCyc; MetaCyc:G6278-MON; -.
DR   UniPathway; UPA00864; UER00832.
DR   PRO; PR:P77161; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008679; F:2-hydroxy-3-oxopropionate reductase activity; IDA:EcoCyc.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0103032; F:tartronate semialdehyde reductase activity; IEA:RHEA.
DR   GO; GO:0009442; P:allantoin assimilation pathway; IEP:EcoCyc.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR   GO; GO:0046296; P:glycolate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009436; P:glyoxylate catabolic process; IMP:EcoCyc.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029154; NADP-bd.
DR   InterPro; IPR006398; Tartro_sem_red.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01505; tartro_sem_red; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..292
FT                   /note="2-hydroxy-3-oxopropionate reductase"
FT                   /id="PRO_0000173061"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000250"
FT   BINDING         4..18
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  30801 MW;  5D5263231F2910F0 CRC64;
     MKLGFIGLGI MGTPMAINLA RAGHQLHVTT IGPVADELLS LGAVSVETAR QVTEASDIIF
     IMVPDTPQVE EVLFGENGCT KASLKGKTIV DMSSISPIET KRFARQVNEL GGDYLDAPVS
     GGEIGAREGT LSIMVGGDEA VFERVKPLFE LLGKNITLVG GNGDGQTCKV ANQIIVALNI
     EAVSEALLFA SKAGADPVRV RQALMGGFAS SRILEVHGER MIKRTFNPGF KIALHQKDLN
     LALQSAKALA LNLPNTATCQ ELFNTCAANG GSQLDHSALV QALELMANHK LA