Reviewed,
UniProtKB/Swiss-Prot P0A9B5 (G3P1_SHIFL)
Last modified
November 25, 2008.
Version 31.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glyceraldehyde-3-phosphate dehydrogenase A Short name=GAPDH-A EC=1.2.1.12 | ||||
| Gene names |
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| Organism | Shigella flexneri [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 623 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella |
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 By similarity. |
| Subcellular location | CytoplasmBy similarity. |
| Sequence similarities | Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NAD binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activityInferred from electronic annotation. Source: InterPro |
| 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 A | PRO_0000145678 | |||||
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 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 132 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 138 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 192 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 249 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. Yu J.Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a. |
| [2] | "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a. |
Cross-references
Sequence databases | |
|---|---|
| AE005674 Genomic DNA. Translation: AAN43042.1. Different initiation. AE014073 Genomic DNA. Translation: AAP16937.1. | |
| RefSeq | NP_707335.2. NP_837130.1. |
3D structure databases | |
| SMR | P0A9B5. Positions 2-331. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1024650. 1077928. |
| GenomeReviews | Gene locus S1559 in contig AE014073_GR. Gene locus SF1444 in contig AE005674_GR. |
| KEGG | sfl:SF1444. sfx:S1559. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0A9B5. |
Enzyme and pathway databases | |
| BioCyc | SFLE198214:AAN43042.1-MON. |
Family and domain databases | |
| InterPro | IPR000173. GlycerAld_3-P_DHase. IPR006424. Glyceraldehyde-3-P_DHase_1. [Graphical view] |
| 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. |
| TIGRFAMs | TIGR01534. GAPDH-I. 1 hit. |
| PROSITE | PS00071. GAPDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | G3P1_SHIFL | ||||||||
| Accession | Primary (citable) accession number: P0A9B5 Secondary accession number(s): P06977 | ||||||||
| 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


