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Protein

Glyoxylate/hydroxypyruvate reductase B

Gene

ghrB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Can also reduce 2,5-diketo-D-gluconate (25DKG) to 5-keto-D-gluconate (5KDG), 2-keto-D-gluconate (2KDG) to D-gluconate, and 2-keto-L-gulonate (2KLG) to L-idonate (IA), but it is not its physiological function. Inactive towards 2-oxoglutarate, oxaloacetate, pyruvate, 5-keto-D-gluconate, D-fructose and L-sorbose. Activity with NAD is very low.

Catalytic activityi

Glycolate + NADP+ = glyoxylate + NADPH.1 Publication
D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H.1 Publication
D-gluconate + NADP+ = 2-dehydro-D-gluconate + NADPH.1 Publication

Kineticsi

The catalytic efficiency is better for hydroxypyruvate than glyoxylate with NADPH as electron donor.

  1. KM=0.7 mM for hydroxypyruvate (at pH 7.5)2 Publications
  2. KM=1.5 mM for 2-oxo-D-gluconate (at pH 7.5)2 Publications
  3. KM=6.6 mM for glyoxylate (at pH 7.5)2 Publications
  1. Vmax=345 µmol/min/mg enzyme with glyoxylate as substrate (at pH 7)2 Publications
  2. Vmax=123 µmol/min/mg enzyme with hydroxypyruvate as substrate (at pH 7)2 Publications
  3. Vmax=69 µmol/min/mg enzyme with 2-oxo-D-gluconate as substrate (at pH 7)2 Publications

pH dependencei

Optimum pH is 7.5.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei237 – 2371By similarity
Active sitei266 – 2661By similarity
Active sitei285 – 2851Proton donorBy similarity

GO - Molecular functioni

  • gluconate 2-dehydrogenase activity Source: EcoCyc
  • glyoxylate reductase (NADP) activity Source: EcoCyc
  • hydroxypyruvate reductase activity Source: GO_Central
  • NAD binding Source: InterPro

GO - Biological processi

  • D-gluconate metabolic process Source: UniProtKB-KW
  • ketogluconate catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Gluconate utilization

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER-43.
ECOL316407:JW5656-MONOMER.
MetaCyc:MONOMER-43.
SABIO-RKP37666.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyoxylate/hydroxypyruvate reductase B (EC:1.1.1.79, EC:1.1.1.81)
Alternative name(s):
2-ketoaldonate reductase
2-ketogluconate reductase (EC:1.1.1.215)
Short name:
2KR
Gene namesi
Name:ghrB
Synonyms:tkrA, yiaE
Ordered Locus Names:b3553, JW5656
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12272. ghrB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • plasma membrane Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Glyoxylate/hydroxypyruvate reductase BPRO_0000076029Add
BLAST

Proteomic databases

EPDiP37666.
PaxDbiP37666.
PRIDEiP37666.

Expressioni

Inductioni

Constitutively expressed.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4259301. 9 interactions.
DIPiDIP-10997N.
IntActiP37666. 1 interaction.
STRINGi511145.b3553.

Structurei

3D structure databases

ProteinModelPortaliP37666.
SMRiP37666. Positions 1-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C5I. Bacteria.
COG1052. LUCA.
HOGENOMiHOG000136700.
InParanoidiP37666.
KOiK00090.
OMAiKSIGPDW.
OrthoDBiEOG6VXFC3.
PhylomeDBiP37666.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_01667. 2_Hacid_dh_C_GhrB.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR006140. D-isomer_DH_NAD-bd.
IPR023756. Glyo/OHPyrv_Rdtase_B.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37666-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPSVILYKA LPDDLLQRLQ EHFTVHQVAN LSPQTVEQNA AIFAEAEGLL
60 70 80 90 100
GSNENVNAAL LEKMPKLRAT STISVGYDNF DVDALTARKI LLMHTPTVLT
110 120 130 140 150
ETVADTLMAL VLSTARRVVE VAERVKAGEW TASIGPDWYG TDVHHKTLGI
160 170 180 190 200
VGMGRIGMAL AQRAHFGFNM PILYNARRHH KEAEERFNAR YCDLDTLLQE
210 220 230 240 250
SDFVCLILPL TDETHHLFGA EQFAKMKSSA IFINAGRGPV VDENALIAAL
260 270 280 290 300
QKGEIHAAGL DVFEQEPLSV DSPLLSMANV VAVPHIGSAT HETRYGMAAC
310 320
AVDNLIDALQ GKVEKNCVNP HVAD
Length:324
Mass (Da):35,396
Last modified:December 15, 1998 - v3
Checksum:i1B21339B1337D255
GO

Sequence cautioni

The sequence AAB18530.1 differs from that shown. Reason: Frameshift at position 324. Curated
The sequence AAB18530.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18530.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76577.2.
AP009048 Genomic DNA. Translation: BAE77742.1.
PIRiC65154.
RefSeqiNP_418009.2. NC_000913.3.
WP_000805038.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76577; AAC76577; b3553.
BAE77742; BAE77742; BAE77742.
GeneIDi948074.
KEGGiecj:JW5656.
eco:b3553.
PATRICi32122578. VBIEscCol129921_3666.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18530.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76577.2.
AP009048 Genomic DNA. Translation: BAE77742.1.
PIRiC65154.
RefSeqiNP_418009.2. NC_000913.3.
WP_000805038.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP37666.
SMRiP37666. Positions 1-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259301. 9 interactions.
DIPiDIP-10997N.
IntActiP37666. 1 interaction.
STRINGi511145.b3553.

Proteomic databases

EPDiP37666.
PaxDbiP37666.
PRIDEiP37666.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76577; AAC76577; b3553.
BAE77742; BAE77742; BAE77742.
GeneIDi948074.
KEGGiecj:JW5656.
eco:b3553.
PATRICi32122578. VBIEscCol129921_3666.

Organism-specific databases

EchoBASEiEB2181.
EcoGeneiEG12272. ghrB.

Phylogenomic databases

eggNOGiENOG4105C5I. Bacteria.
COG1052. LUCA.
HOGENOMiHOG000136700.
InParanoidiP37666.
KOiK00090.
OMAiKSIGPDW.
OrthoDBiEOG6VXFC3.
PhylomeDBiP37666.

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER-43.
ECOL316407:JW5656-MONOMER.
MetaCyc:MONOMER-43.
SABIO-RKP37666.

Miscellaneous databases

PROiP37666.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_01667. 2_Hacid_dh_C_GhrB.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR006140. D-isomer_DH_NAD-bd.
IPR023756. Glyo/OHPyrv_Rdtase_B.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO C-TERMINUS.
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The yiaE gene, located at 80.1 minutes on the Escherichia coli chromosome, encodes a 2-ketoaldonate reductase."
    Yum D.-Y., Lee B.-Y., Hahm D.-H., Pan J.-G.
    J. Bacteriol. 180:5984-5988(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-22, SUBUNIT, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-8.
    Strain: K12 / EMG2.
  6. "Biochemical characterization of the 2-ketoacid reductases encoded by ycdW and yiaE genes in Escherichia coli."
    Nunez M.F., Pellicer M.T., Badia J., Aguilar J., Baldoma L.
    Biochem. J. 354:707-715(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

Entry informationi

Entry nameiGHRB_ECOLI
AccessioniPrimary (citable) accession number: P37666
Secondary accession number(s): Q2M7L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: December 15, 1998
Last modified: July 6, 2016
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.