[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; DNA Res. 3:137-155(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[4]	PROTEIN SEQUENCE OF 1-10, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES. STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; DOI=10.1042/0264-6021:3540707; PubMed=11237876 [NCBI, ExPASy, EBI, Israel, Japan] Nunez M.F., Pellicer M.T., Badia J., Aguilar J., Baldoma L.; "Biochemical characterization of the 2-ketoacid reductases encoded by ycdW and yiaE genes in Escherichia coli."; Biochem. J. 354:707-715(2001).
[5]	IDENTIFICATION BY MASS SPECTROMETRY. DOI=10.1002/(SICI)1522-2683(19990801)20:11<2181::AID-ELPS2181>3.3.CO;2-H; PubMed=10493123 [NCBI, ExPASy, EBI, Israel, Japan] Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.; "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."; Electrophoresis 20:2181-2195(1999).

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.
CATALYTIC ACTIVITY: Glycolate + NADP⁺ = glyoxylate + NADPH.
CATALYTIC ACTIVITY: D-glycerate + NAD(P)⁺ = hydroxypyruvate + NAD(P)H.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=0.6 mM for glyoxylate (at 25 degrees Celsius and pH 7);
	K_M=1.0 mM for hydroxypyruvate (at 25 degrees Celsius and pH 7);
	V_max=120 µmol/min/mg enzyme with glyoxylate as substrate (at 25 degrees Celsius and pH 7);
	V_max=20 µmol/min/mg enzyme with hydroxypyruvate as substrate (at 25 degrees Celsius and pH 7);
	Note=The catalytic efficiency is better for glyoxylate than hydroxypyruvate with NADPH as electron donor;
pH dependence:	Optimum pH is 7.0;

SUBCELLULAR LOCATION: Cytoplasm (Probable).
INDUCTION: Constitutively expressed.
SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrA subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U00096; AAC74117.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35814.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F64845; F64845.

RefSeq

AP_001658.1; -.
NP_415551.2; -.

3D structure databases

ModBase

P75913.

Enzyme and pathway databases

BioCyc

EcoCyc:G6539-MON; -.
MetaCyc:G6539-MON; -.

Organism-specific databases

EchoBASE

EB3628; -.

EcoGene

EG13869; ghrA.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0030267;	Molecular function: glyoxylate reductase (NADP) activity (inferred from electronic annotation from HAMAP).
GO:0016618;	Molecular function: hydroxypyruvate reductase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01666; -; 1.
PBIL [Tree]

InterPro

IPR006140; D-isomer_2_OHA_DHase_NAD-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF02826; 2-Hacid_dh_C; 1.
Pfam graphical view of domain structure.

PROSITE

PS00065; D_2_HYDROXYACID_DH_1; FALSE_NEG.
PS00670; D_2_HYDROXYACID_DH_2; FALSE_NEG.
PS00671; D_2_HYDROXYACID_DH_3; 1.

Genome annotation databases

GeneID

946431; -.

GenomeReviews

U00096_GR; b1033.
AP009048_GR; JW5146.

KEGG

ecj:JW5146; -.
eco:b1033; -.

Phylogenomic databases

HOGENOM

P75913; -.

Genome annotation databases

CMR

P75913; b1033.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Direct protein sequencing; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 312`	`312`	`Glyoxylate/hydroxypyruvate reductase A.`	`PRO_0000076028`
`ACT_SITE`	`227 227`		`By similarity.`
`ACT_SITE`	`275 275`		`Proton donor (By similarity).`

Sequence information

Length: 312 AA [This is the length of the unprocessed precursor]

Molecular weight: 35343 Da [This is the MW of the unprocessed precursor]

CRC64: 5B2F966D11DC6B40 [This is a checksum on the sequence]

        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

P75913 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools