Reviewed, UniProtKB/Swiss-Prot P58000 (GHRB_ENTAG)

Names and origin

Protein names

Recommended name:
    Glyoxylate/hydroxypyruvate reductase B
    EC=1.1.1.79
    EC=1.1.1.81

Gene names

Name:

tkrA

Organism

Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)

Taxonomic identifier

549 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pantoea

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively By similarity.
Catalytic activity	Glycolate + NADP+ = glyoxylate + NADPH. HAMAP MF_01667 D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H. HAMAP MF_01667
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glyoxylate reductase (NADP) activity Inferred from electronic annotation. Source: HAMAP hydroxypyruvate reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 323	323	Glyoxylate/hydroxypyruvate reductase B HAMAP MF_01667		PRO_0000076031
Sites
	Active site	236	1	By similarity
	Active site	265	1	By similarity
	Active site	284	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P58000-1 [UniParc]. Last modified April 27, 2001. Version 1. Checksum: BD778BDFDDF53AD1	FASTA	323	35,336
	10 20 30 40 50 60 MKPEVLLYKS LPDDLRARLD EHFTVTAING LSPETIAEHG GAGARRRHDR LQQHGGSSAA 70 80 90 100 110 120 GENAKLRAAS TISVGYDNFD VEALNQRGIV LIDTPTVLTE TVADTMMALV LSSARRVVEV 130 140 150 160 170 180 AERVKAGEWR RSIGPDWFGI DVHHKKMGIL GMGRIGLALA QRAHHGFGMP ILYNARKHHE 190 200 210 220 230 240 EAESRFNAQY CDLDTLLRES DFLCISLPLT EQTHHMIGRE QLAKMKPSAI LINAGRGPVV 250 260 270 280 290 300 DEQALIAALK DKTIHAAGLD VFEQEPLPVD SELLTLPNVV ALPHIGSATH ETRYGMARDA 310 320 VDNLIAALAG KVEKNCVNPQ VLR

References

[1]	"Metabolic pathway engineering to increase production of ascorbic acid intermediates." Anderson S., Lazarus R.A., Miller H.I., Stafford R.K. Patent number US5032514, 16-JUL-1991 Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: ATCC 21998 / FERM P-2439.

Cross-references

3D structure databases
HSSP	HSSP built from PDB template 1GDH based on UniProtKB P36234.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.215. 3054.
Family and domain databases
HAMAP	MF_01667. [Tree]
InterPro	IPR006139. D-isomer_2_OHA_DH. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. [Graphical view]
PROSITE	PS00065. D_2_HYDROXYACID_DH_1. False negative. PS00670. D_2_HYDROXYACID_DH_2. False negative. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GHRB_ENTAG

Accession

Primary (citable) accession number: P58000

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	April 27, 2001
Last modified:	June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)