Q4MQ58 (G3P1_BACCE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 38.
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 1 Short name=GAPDH 1 EC=1.2.1.12 | ||||
| Gene names |
| ||||
| 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. Ref.2 |
| 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 |
| 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 Ref.2 | ||||||
| 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 UniProtKB P00362 | ||||||
Sites | |||||||||
| Active site | 151 | 1 | Nucleophile By similarity UniProtKB P00362 | ||||||
| Binding site | 33 | 1 | NAD By similarity UniProtKB P00362 | ||||||
| Binding site | 77 | 1 | NAD; via carbonyl oxygen By similarity UniProtKB P00362 | ||||||
| Binding site | 119 | 1 | NAD By similarity UniProtKB P00362 | ||||||
| Binding site | 181 | 1 | Glyceraldehyde 3-phosphate By similarity UniProtKB P00362 | ||||||
| Binding site | 196 | 1 | Glyceraldehyde 3-phosphate By similarity UniProtKB P00362 | ||||||
| Binding site | 232 | 1 | Glyceraldehyde 3-phosphate By similarity UniProtKB P00362 | ||||||
| Binding site | 314 | 1 | NAD By similarity UniProtKB P00362 | ||||||
| Site | 178 | 1 | Activates thiol group during catalysis By similarity UniProtKB P00362 | ||||||
Experimental info | |||||||||
| Sequence conflict | 13 | 1 | G → R AA sequence Ref.2 | ||||||
Sequences
| ||||||||||||||||||
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 | |
|---|---|
| EMBL GenBank DDBJ | AAEK01000016 Genomic DNA. Translation: EAL14305.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NQO based on UniProtKB P00362. |
| ProteinModelPortal | Q4MQ58. |
| SMR | Q4MQ58. Positions 3-334. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| PATRIC | 24957964. VBIBacCer116370_2912. |
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. |
| 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_BACCE | ||||||||
| Accession | Primary (citable) accession number: Q4MQ58 Secondary accession number(s): P83078 | ||||||||
| Entry history |
| ||||||||
| 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 |

Clusters with