[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.; Submitted (NOV-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

CP000886; ABX67784.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001588616.1; -.

3D structure databases

ModBase

A9N5T3.

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:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
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

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

Gene3D

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

PROSITE

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

ProtoNet

A9N5T3.

Genome annotation databases

GeneID

5780893; -.

GenomeReviews

CP000886_GR; SPAB_02402.

KEGG

spq:SPAB_02402; -.

CMR

A9N5T3; SPAB_02402.

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_0000348370`
`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: 34947 Da [This is the MW of the unprocessed precursor]

CRC64: 26788E045AB2450E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEIIFYHPTF NAAWWVNALE KALPHARVRE WKVGDNNPAD YALVWQPPVE MLAGRRLKAV 

        70         80         90        100        110        120 
FALGAGVDAI LSKLNAHPEM LDASIPLFRL EDTGMGLQMQ EYAVSQVLHW FRRFDDYQAL 

       130        140        150        160        170        180 
KNQALWKPLP EYTREEFSVG IMGAGVLGAK VAESLQAWGF PLRCWSRSRK SWPGVESYVG 

       190        200        210        220        230        240 
REELHAFLNQ TRVLINLLPN TAQTVGIINS ELLDQLPDGA YVLNLARGVH VQEADLLAAL 

       250        260        270        280        290        300 
DSGKLKGAML DVFSQEPLPQ ESPLWRHPRV AMTPHIAAVT RPAEAIDYIS RTIAQLEKGE 

       310 
SVTGQVDRAR GY

A9N5T3 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