P0A1P0 (G3P1_SALTY) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 57.
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 Short name=GAPDH EC=1.2.1.12 | ||||||
| Gene names |
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| Organism | Salmonella typhimurium | ||||||
| Taxonomic identifier | 90371 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 331 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Sequence similarities | Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| 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+) (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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 331 | 330 | Glyceraldehyde-3-phosphate dehydrogenase | PRO_0000145677 | |||||
Regions | |||||||||
| Nucleotide binding | 12 – 13 | 2 | NAD By similarity | ||||||
| Region | 149 – 151 | 3 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
| Region | 209 – 210 | 2 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
Sites | |||||||||
| Active site | 150 | 1 | Nucleophile By similarity | ||||||
| Binding site | 34 | 1 | NAD By similarity | ||||||
| Binding site | 78 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 180 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 232 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 314 | 1 | NAD By similarity | ||||||
| Site | 177 | 1 | Activates thiol group during catalysis By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 95 | 1 | E → D in AAA27114. Ref.2 | ||||||
| Sequence conflict | 98 | 1 | G → V in AAA27114. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K.Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720. |
| [2] | "Molecular and evolutionary relationships among enteric bacteria." Lawrence J.G., Ochman H., Hartl D.L. J. Gen. Microbiol. 137:1911-1921(1991) [PubMed: 1955870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-309. Strain: LT2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE006468 Genomic DNA. Translation: AAL20215.1. M63369 Genomic DNA. Translation: AAA27114.1. |
| RefSeq | NP_460256.1. NC_003197.1. |
3D structure databases | |
| ProteinModelPortal | P0A1P0. |
| SMR | P0A1P0. Positions 2-331. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P0A1P0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1252808. |
| GenomeReviews | Gene locus STM1290 in contig AE006468_GR. |
| KEGG | stm:STM1290. |
| PATRIC | 32381057. VBISalEnt20916_1371. |
Phylogenomic databases | |
| HOGENOM | HBG571736. |
| OMA | DARTSIF. |
| ProtClustDB | PRK15425. |
Enzyme and pathway databases | |
| BioCyc | STYP99287:STM1290-MONOMER. |
Family and domain databases | |
| 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] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00134. |
| PANTHER | PTHR10836. GAP_DH. 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 | G3P1_SALTY | ||||||||
| Accession | Primary (citable) accession number: P0A1P0 Secondary accession number(s): P24165 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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