Reviewed, UniProtKB/Swiss-Prot P75913 (GHRA_ECOLI)

Names and origin

Protein names

Recommended name:
    Glyoxylate/hydroxypyruvate reductase A
    EC=1.1.1.79
    EC=1.1.1.81
Alternative name(s):
    2-ketoacid reductase

Gene names

Name:	ghrA
Synonyms:	ycdW
Ordered Locus Names:	b1033, JW5146

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Inactive towards 2-oxo-D-gluconate, 2-oxoglutarate, oxaloacetate and pyruvate. Only D- and L-glycerate are involved in the oxidative activity with NADP. Activity with NAD is very low. HAMAP MF_01666
Catalytic activity	Glycolate + NADP+ = glyoxylate + NADPH. Ref.4 D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H. Ref.4
Subcellular location	Cytoplasm Probable.
Induction	Constitutively expressed. Ref.4
Sequence similarities	Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrA subfamily.
biophysicochemical properties	Kinetic parameters: The catalytic efficiency is better for glyoxylate than hydroxypyruvate with NADPH as electron donor. KM=0.6 mM for glyoxylate (at 25 degrees Celsius and pH 7) HAMAP MF_01666 KM=1.0 mM for hydroxypyruvate (at 25 degrees Celsius and pH 7) Vmax=120 µmol/min/mg enzyme with glyoxylate as substrate (at 25 degrees Celsius and pH 7) Vmax=20 µmol/min/mg enzyme with hydroxypyruvate as substrate (at 25 degrees Celsius and pH 7) pH dependence: Optimum pH is 7.0.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	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	cofactor binding Inferred from electronic annotation. Source: InterPro glyoxylate reductase (NADP) activity Inferred from electronic annotation. Source: HAMAP hydroxypyruvate reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 312	312	Glyoxylate/hydroxypyruvate reductase A HAMAP MF_01666		PRO_0000076028
Sites
	Active site	227	1	By similarity
	Active site	275	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P75913-1 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 5B2F966D11DC6B40	FASTA	312	35,343
	10 20 30 40 50 60 MDIIFYHPTF DTQWWIEALR KAIPQARVRA WKSGDNDSAD YALVWHPPVE MLAGRDLKAV 70 80 90 100 110 120 FALGAGVDSI LSKLQAHPEM LNPSVPLFRL EDTGMGEQMQ EYAVSQVLHW FRRFDDYRIQ 130 140 150 160 170 180 QNSSHWQPLP EYHREDFTIG ILGAGVLGSK VAQSLQTWRF PLRCWSRTRK SWPGVQSFAG 190 200 210 220 230 240 REELSAFLSQ CRVLINLLPN TPETVGIINQ QLLEKLPDGA YLLNLARGVH VVEDDLLAAL 250 260 270 280 290 300 DSGKVKGAML DVFNREPLPP ESPLWQHPRV TITPHVAAIT RPAEAVEYIS RTIAQLEKGE 310 RVCGQVDRAR GY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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]. 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]	"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: PROTEIN SEQUENCE OF 1-10, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[5]	"Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography." Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B. Electrophoresis 20:2181-2195(1999) [PubMed: 10493123] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00096 Genomic DNA. Translation: AAC74117.2. AP009048 Genomic DNA. Translation: BAA35814.1.
PIR	F64845.
RefSeq	AP_001658.1. NP_415551.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	946431.
GenomeReviews	Gene locus JW5146 in contig AP009048_GR. Gene locus b1033 in contig U00096_GR.
KEGG	ecj:JW5146. eco:b1033.
Organism-specific databases
EchoBASE	EB3628.
EcoGene	EG13869. ghrA.
CMR	Search...
Phylogenomic databases
HOGENOM	P75913.
OMA	P75913. YALVWRA.
Enzyme and pathway databases
BioCyc	EcoCyc:G6539-MON. MetaCyc:G6539-MON.
Family and domain databases
HAMAP	MF_01666. [Tree]
InterPro	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	PF02826. 2-Hacid_dh_C. 1 hit. [Graphical view]
PROSITE	PS00065. D_2_HYDROXYACID_DH_1. False negative. PS00670. D_2_HYDROXYACID_DH_2. False negative. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GHRA_ECOLI

Accession

Primary (citable) accession number: P75913
Secondary accession number(s): Q9R3M8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 13, 2007
Last modified:	June 16, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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