Reviewed,
UniProtKB/Swiss-Prot Q59516 (DHGY_METEX)
Last modified
June 16, 2009.
Version 60.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
| ||
| 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 | |
| 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 activityInferred 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
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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 | |
|---|---|
| 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 |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


