O34425 (G3P2_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 110.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glyceraldehyde-3-phosphate dehydrogenase 2 EC=1.2.1.59 Alternative name(s): NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase Short name=GAPDH | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 224308 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 340 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | More active in anabolism. |
| Catalytic activity | D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. |
| Biophysicochemical properties | Kinetic parameters: The catalytic efficiency is 50-fold higher with NADP than with NAD. KM=5.7 mM for NAD KM=0.86 mM for NADP |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | NAD binding Inferred from electronic annotation. Source: InterPro NADP bindingInferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 340 | 340 | Glyceraldehyde-3-phosphate dehydrogenase 2 | PRO_0000145635 | |||||
Regions | |||||||||
| Nucleotide binding | 12 – 13 | 2 | NAD By similarity | ||||||
| Region | 151 – 153 | 3 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
| Region | 210 – 211 | 2 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
Sites | |||||||||
| Active site | 152 | 1 | Nucleophile By similarity | ||||||
| Binding site | 78 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 182 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 197 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 233 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 315 | 1 | NAD By similarity | ||||||
| Site | 179 | 1 | Activates thiol group during catalysis By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium." Fillinger S., Boschi-Muller S., Azza S., Dervyn E., Branlant G., Aymerich S. J. Biol. Chem. 275:14031-14037(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF008220 Genomic DNA. Translation: AAC00355.1. AL009126 Genomic DNA. Translation: CAB14862.1. |
| PIR | G69628. |
| RefSeq | NP_390780.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | O34425. |
| SMR | O34425. Positions 3-333. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU29020. |
Proteomic databases | |
| PaxDb | O34425. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB14862; CAB14862; BSU29020. |
| GeneID | 937393. |
| KEGG | bsu:BSU29020. |
| PATRIC | 18977696. VBIBacSub10457_3036. |
Organism-specific databases | |
| GenoList | BSU29020. [Micado] |
Phylogenomic databases | |
| eggNOG | COG0057. |
| HOGENOM | HOG000071679. |
| KO | K00134. |
| OMA | NDQNNID. |
| ProtClustDB | PRK07729. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU29020-MONOMER. |
| SABIO-RK | O34425. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| InterPro | IPR020831. GlycerAld/Erythrose_P_DH. IPR020830. GlycerAld_3-P_DH_AS. IPR020829. GlycerAld_3-P_DH_cat. IPR020828. GlycerAld_3-P_DH_NAD(P)-bd. IPR006424. Glyceraldehyde-3-P_DH_1. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PANTHER | PTHR10836. PTHR10836. 1 hit. |
| Pfam | PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000149. GAP_DH. 1 hit. |
| PRINTS | PR00078. G3PDHDRGNASE. |
| SMART | SM00846. Gp_dh_N. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01534. GAPDH-I. 1 hit. |
| PROSITE | PS00071. GAPDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | G3P2_BACSU | ||||||||
| Accession | Primary (citable) accession number: O34425 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with
