[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Improved long green; TISSUE=Cotyledon; DOI=10.1007/BF00016133; PubMed=2519111 [NCBI, ExPASy, EBI, Israel, Japan] Greenler J.M., Sloan J.S., Schwartz B.W., Becker W.M.; "Isolation, characterization and sequence analysis of a full-length cDNA clone encoding NADH-dependent hydroxypyruvate reductase from cucumber."; Plant Mol. Biol. 13:139-150(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Wisconsin 2238G; DOI=10.1007/BF00037078; PubMed=1912510 [NCBI, ExPASy, EBI, Israel, Japan] Schwartz B.W., Sloan J.S., Becker W.M.; "Characterization of genes encoding hydroxypyruvate reductase in cucumber."; Plant Mol. Biol. 17:941-947(1991).

Comments

CATALYTIC ACTIVITY: (R)-glycerate + NAD⁺ = hydroxypyruvate + NADH.
PATHWAY: Photosynthesis; photorespiration; 3-phospho-D-glyceric acid from glycine: step 3/4 .
SUBCELLULAR LOCATION: Peroxisome.
INDUCTION: The appearance of HPR in the cotyledons of cucumber seedlings is both developmentally and light-regulated possibly at the level of transcription.
SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

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

X14609; CAA32764.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X58542; CAA41434.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S17733; DEKVG.

3D structure databases

HSSP

P30901; 2DLD. [HSSP ENTRY / PDB]

ModBase

P13443.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0008465;	Molecular function: glycerate dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009854;	Biological process: oxidative photosynthetic carbon pathway (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006139; D-isomer_2_OHA_DHase.
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

PF00389; 2-Hacid_dh; 1.
PF02826; 2-Hacid_dh_C; 1.
Pfam graphical view of domain structure.

PROSITE

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

Other

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

Keywords

Glycolate pathway; NAD; Oxidoreductase; Peroxisome; Photorespiration.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 382`	`382`	`Glycerate dehydrogenase.`	`PRO_0000075941`
`ACT_SITE`	`273 273`		`By similarity.`
`ACT_SITE`	`302 302`		`By similarity.`
`ACT_SITE`	`320 320`		`Proton donor (By similarity).`

Sequence information

Length: 382 AA [This is the length of the unprocessed precursor]

Molecular weight: 41706 Da [This is the MW of the unprocessed precursor]

CRC64: 4E326485ACD0E080 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKPVQIEVW NPNGKYRVVS TKPMPGTRWI NLLIEQDCRV EICTEKKTIL SVEDILALIG 

        70         80         90        100        110        120 
DKCDGVIGQL TEDWGEVLFS ALSRAGGKAF SNMAVGYNNV DVNAANKYGV AVGNTPGVLT 

       130        140        150        160        170        180 
ETTAELAASL SLAAARRIVE ADEFMRAGRY DGWLPNLFVG NLLKGQTVGV IGAGRIGSAY 

       190        200        210        220        230        240 
ARMMVEGFKM NLIYFDLYQS TRLEKFVTAY GEFLKANGEA PVTWRRASSM DEVLREADVI 

       250        260        270        280        290        300 
SLHPVLDKTT FHLVNKESLK AMKKDAILIN CSRGPVIDEA ALVDHLRDNP MFRVGLDVFE 

       310        320        330        340        350        360 
DEPYMKPGLA DMKNAIIVPH IASASKWTRE GMATLAALNV LGKIKGYPVW SDPNRVEPFL 

       370        380 
DENVSPPAAS PSIVNAKALG NA

P13443 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