Reviewed,
UniProtKB/Swiss-Prot Q4MQ58 (G3P1_BACCE)
Last modified
November 25, 2008.
Version 19.
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 1 Short name=GAPDH 1 EC=1.2.1.12 | ||||
| Gene names |
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| Organism | Bacillus cereus | ||||
| Taxonomic identifier | 1396 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 334 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)
| 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 | |
| Induction | Repressed by salt stress. |
| 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 | Direct protein sequencing |
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 | ||||||
| Chain | 2 – 334 | 333 | Glyceraldehyde-3-phosphate dehydrogenase 1 | PRO_0000271247 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 12 | 2 | NAD By similarity | ||||||
| Region | 150 – 152 | 3 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
Sites | |||||||||
| Active site | 151 | 1 | Nucleophile By similarity | ||||||
| Binding site | 33 | 1 | NAD By similarity | ||||||
| Binding site | 77 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 119 | 1 | NAD By similarity | ||||||
| Binding site | 181 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 196 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 232 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 314 | 1 | NAD By similarity | ||||||
| Site | 178 | 1 | Activates thiol group during catalysis By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 13 | 1 | G → R AA sequence Ref.2 | ||||||
Sequences
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References
| [1] | "Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax." Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D., Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W., Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J., Peterson S.N., Weyant R.S. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004) [PubMed: 15155910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G9241. |
| [2] | "Heat and salt stress in the food pathogen Bacillus cereus." Browne N., Dowds B.C.A. J. Appl. Microbiol. 91:1085-1094(2001) [PubMed: 11851817] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21, INDUCTION. Strain: NCIMB 11796 / DSM 626. |
Cross-references
Sequence databases | |
|---|---|
| AAEK01000016 Genomic DNA. Translation: EAL14305.1. | |
3D structure databases | |
| SMR | Q4MQ58. Positions 3-334. |
| ModBase | Search... |
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_BACCE | ||||||||
| Accession | Primary (citable) accession number: Q4MQ58 Secondary accession number(s): P83078 | ||||||||
| 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


