[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.; "Complete sequence of Escherichia coli SECEC SMS-3-5."; Submitted (MAR-2008) 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.
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB 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

CP000970; ACB16053.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001745839.1; -.

3D structure databases

ModBase

B1LJB3.

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:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01667; -; 1.
PBIL [Tree]

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

Genome annotation databases

GeneID

6145008; -.

GenomeReviews

CP000970_GR; EcSMS35_3874.

KEGG

ecm:EcSMS35_3874; -.

CMR

B1LJB3; EcSMS35_3874.

Other

ProtoNet

B1LJB3.

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`	`1 324`	`324`	`Glyoxylate/hydroxypyruvate reductase B.`	`PRO_0000348385`
`ACT_SITE`	`237 237`		`By similarity.`
`ACT_SITE`	`266 266`		`By similarity.`
`ACT_SITE`	`285 285`		`Proton donor (By similarity).`

Sequence information

Length: 324 AA [This is the length of the unprocessed precursor]

Molecular weight: 35387 Da [This is the MW of the unprocessed precursor]

CRC64: 26A5ACFD218B903A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKPSVILYKA LPDDLLQRLQ EHFTVHQVAN LSPQTVEQNA AIFAEAEGLL GSNENVDAAL 

        70         80         90        100        110        120 
LEKMPKLRAT STISVGYDNF DVDALTARKI LLMHTPTVLT ETVADTLMAL VLSTARRVVE 

       130        140        150        160        170        180 
VAERVKAGEW TASIGPDWYG TDVHHKTLGI VGMGRIGMAL AQRAQFGFNM PILYNARRHH 

       190        200        210        220        230        240 
KEAEERFNAR YCDLDTLLQE SDFVCLILPL TDETHHLFGA EQFAKMKSSA IFINAGRGPV 

       250        260        270        280        290        300 
VDENALIAAL QKGEIHAAGL DVFEQEPLSV DSPLLSMANV VAVPHIGSAT HETRYGMAAC 

       310        320 
AVDNLIDALQ GKVEKNCVNP HVAD

B1LJB3 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