Reviewed, UniProtKB/Swiss-Prot Q59516 (DHGY_METEX)

Names and origin

Protein names

Recommended name:
    Glycerate dehydrogenase
      Short name=GDH
    EC=1.1.1.29
Alternative name(s):
    NADH-dependent hydroxypyruvate reductase
      Short name=HPR
      Short name=HPR-A
    Hydroxypyruvate dehydrogenase
    Glyoxylate reductase

Gene names

Name:

hprA

Organism

Methylobacterium extorquens (Protomonas extorquens)

Taxonomic identifier

408 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a central role in assimilation of carbon. It converts hydroxypyruvate to glycerate as a key step in the serine cycle, and may also play an important role in C2 reactions, by interconverting glyoxylate and glycolate.
Catalytic activity	(R)-glycerate + NAD+ = hydroxypyruvate + NADH.
Pathway	One-carbon metabolism; formaldehyde assimilation via serine pathway.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Miscellaneous	Uses both NAD and NADP.
Sequence similarities	Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glycerate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 314	313	Glycerate dehydrogenase		PRO_0000075943
Sites
	Active site	230	1	By similarity
	Active site	259	1	By similarity
	Active site	280	1	Proton donor By similarity
Experimental info
	Sequence conflict	22	1	F → N AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q59516-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B2711E02520A5144	FASTA	314	34,269
	10 20 30 40 50 60 MTKKVVFLDR ESLDATVREF NFPHEYKEYE STWTPEEIVE RLQGAEIAMI NKVPMRADTL 70 80 90 100 110 120 KQLPDLKLIA VAATGTDVVD KAAAKAQGIT VVNIRNYAFN TVPEHVVGLM FALRRAIVPY 130 140 150 160 170 180 ANSVRRGDWN KSKQFCYFDY PIYDIAGSTL GIIGYGALGK SIAKRAEALG MKVLAFDVFP 190 200 210 220 230 240 QDGLVDLETI LTQSDVITLH VPLTPDTKNM IGAEQLKKMK RSAILINTAR GGLVDEAALL 250 260 270 280 290 300 QALKDGTIGG AGFDVVAQEP PKDGNILCDA DLPNLIVTPH VAWASKEAMQ ILADQLVDNV 310 EAFVAGKPQN VVEA

References

[1]	"Genetics of the serine cycle in Methylobacterium extorquens AM1: identification of sgaA and mtdA and sequences of sgaA, hprA, and mtdA." Chistoserdova L.V., Lidstrom M.E. J. Bacteriol. 176:1957-1968(1994) [PubMed: 8144463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AM1 / NCIMB 9133.
[2]	"Cloning, mutagenesis, and physiological effect of a hydroxypyruvate reductase gene from Methylobacterium extorquens AM1." Chistoserdova L.V., Lidstrom M.E. J. Bacteriol. 174:71-77(1992) [PubMed: 1729225] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20. Strain: AM1 / NCIMB 9133.
[3]	"Purification and characterization of hydroxypyruvate reductase from the facultative methylotroph Methylobacterium extorquens AM1." Chistoserdova L.V., Lidstrom M.E. J. Bacteriol. 173:7228-7232(1991) [PubMed: 1657886] [Abstract] Cited for: PROTEIN SEQUENCE OF 3-24, CHARACTERIZATION. Strain: AM1 / NCIMB 9133.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L27235 Genomic DNA. No translation available. M81443 Genomic DNA. Translation: AAA25378.1.
PIR	A44921.
3D structure databases
HSSP	HSSP built from PDB template 1PSD based on UniProtKB P08328.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MON-3821.
BRENDA	1.1.1.29. 20440.
Family and domain databases
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. 1 hit. PS00670. D_2_HYDROXYACID_DH_2. 1 hit. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHGY_METEX

Accession

Primary (citable) accession number: Q59516

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 60 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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