[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Rasko D.A., Rosovitz M.J., Kaper J.B., Nataro J.P., Myers G.S.A., Seshadri R., Cer R.Z., Ravel J.; Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively (By similarity).
CATALYTIC ACTIVITY: Glycolate + NADP⁺ = glyoxylate + NADPH.
CATALYTIC ACTIVITY: D-glycerate + NAD(P)⁺ = hydroxypyruvate + NAD(P)H.
SUBCELLULAR LOCATION: Cytoplasm (Probable).
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

CP000802; ABV05490.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001457873.1; -.

3D structure databases

ModBase

A7ZYY6.

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

5591305; -.

GenomeReviews

CP000802_GR; EcHS_A1151.

KEGG

ecx:EcHS_A1151; -.

CMR

A7ZYY6; EcHS_A1151.

Other

UniRef

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

Keywords

Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 312`	`312`	`Glyoxylate/hydroxypyruvate reductase A.`	`PRO_0000348356`
`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: 35315 Da [This is the MW of the unprocessed precursor]

CRC64: 5B2F96722CDC6B40 [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 
KVCGQVDRAR GY

A7ZYY6 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