Reviewed, UniProtKB/Swiss-Prot P37666 (GHRB_ECOLI)

Names and origin

Protein names

Recommended name:
    Glyoxylate/hydroxypyruvate reductase B
    EC=1.1.1.79
    EC=1.1.1.81
Alternative name(s):
    2-ketogluconate reductase
      Short name=2KR
    EC=1.1.1.215
    2-ketoaldonate reductase

Gene names

Name:	ghrB
Synonyms:	tkrA, yiaE
Ordered Locus Names:	b3553, JW5656

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. HAMAP MF_01667
Catalytic activity	Glycolate + NADP+ = glyoxylate + NADPH. Ref.6 D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H. Ref.6 D-gluconate + NADP+ = 2-dehydro-D-gluconate + NADPH. Ref.6
Subunit structure	Homodimer. Ref.4
Subcellular location	Cytoplasm Probable HAMAP MF_01667.
Induction	Constitutively expressed. Ref.6
Sequence similarities	Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily.
Biophysicochemical properties	Kinetic parameters: The catalytic efficiency is better for hydroxypyruvate than glyoxylate with NADPH as electron donor. KM=0.7 mM for hydroxypyruvate (at pH 7.5) HAMAP MF_01667 KM=1.5 mM for 2-oxo-D-gluconate (at pH 7.5) KM=6.6 mM for glyoxylate (at pH 7.5) Vmax=345 µmol/min/mg enzyme with glyoxylate as substrate (at pH 7) Vmax=123 µmol/min/mg enzyme with hydroxypyruvate as substrate (at pH 7) Vmax=69 µmol/min/mg enzyme with 2-oxo-D-gluconate as substrate (at pH 7) pH dependence: Optimum pH is 7.5.

Ontologies

Keywords
Biological process	Gluconate utilization
Cellular component	Cytoplasm
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	D-gluconate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro gluconate 2-dehydrogenase activity Inferred from electronic annotation. Source: EC glyoxylate reductase (NADP) activity Inferred from electronic annotation. Source: HAMAP hydroxypyruvate reductase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
pgm	P36938	1	EBI-562547,EBI-542427

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 324	324	Glyoxylate/hydroxypyruvate reductase B HAMAP MF_01667		PRO_0000076029
Sites
	Active site	237	1	By similarity
	Active site	266	1	By similarity
	Active site	285	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37666-1 [UniParc]. Last modified December 15, 1998. Version 3. Checksum: 1B21339B1337D255	FASTA	324	35,396
	10 20 30 40 50 60 MKPSVILYKA LPDDLLQRLQ EHFTVHQVAN LSPQTVEQNA AIFAEAEGLL GSNENVNAAL 70 80 90 100 110 120 LEKMPKLRAT STISVGYDNF DVDALTARKI LLMHTPTVLT ETVADTLMAL VLSTARRVVE 130 140 150 160 170 180 VAERVKAGEW TASIGPDWYG TDVHHKTLGI VGMGRIGMAL AQRAHFGFNM PILYNARRHH 190 200 210 220 230 240 KEAEERFNAR YCDLDTLLQE SDFVCLILPL TDETHHLFGA EQFAKMKSSA IFINAGRGPV 250 260 270 280 290 300 VDENALIAAL QKGEIHAAGL DVFEQEPLSV DSPLLSMANV VAVPHIGSAT HETRYGMAAC 310 320 AVDNLIDALQ GKVEKNCVNP HVAD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8041620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 9811658] [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: 9298646] [Abstract] Cited for: PARTIAL 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: 11237876] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00039 Genomic DNA. Translation: AAB18530.1. Frameshift. U00096 Genomic DNA. Translation: AAC76577.1. Different initiation. AP009048 Genomic DNA. Translation: BAE77742.1.
PIR	C65154.
RefSeq	AP_004241.1. NP_418009.2.
3D structure databases
SMR	P37666. Positions 1-323.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10997N.
IntAct	P37666. 1 interaction.
STRING	P37666.
Genome annotation databases
GeneID	948074.
GenomeReviews	Gene locus JW5656 in contig AP009048_GR. Gene locus b3553 in contig U00096_GR.
KEGG	ecj:JW5656. eco:b3553.
Organism-specific databases
EchoBASE	EB2181.
EcoGene	EG12272. ghrB.
CMR	Search...
Phylogenomic databases
eggNOG	COG1052.
HOGENOM	HBG731446.
OMA	KSIGPDW.
Enzyme and pathway databases
BioCyc	EcoCyc:MONOMER-43. ECOL168927:B3553-MONOMER. MetaCyc:MONOMER-43.
Gene expression databases
Genevestigator	P37666.
Family and domain databases
HAMAP	MF_01667. 2-Hacid_dh_C_GhrB. [Tree]
InterPro	IPR006139. D-isomer_2_OHA_DH_cat_dom. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. [Graphical view]
PROSITE	PS00065. D_2_HYDROXYACID_DH_1. False negative. PS00670. D_2_HYDROXYACID_DH_2. 1 hit. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GHRB_ECOLI

Accession

Primary (citable) accession number: P37666
Secondary accession number(s): Q2M7L4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	December 15, 1998
Last modified:	January 19, 2010
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)