P46713 (G3P_MYCLE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 86.
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 | Mycobacterium leprae [Complete proteome] [HAMAP] | ||||||||
| Taxonomic identifier | 1769 [NCBI] | ||||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 339 AA. |
| Sequence status | Complete. |
| 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 | |
| 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 |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 339 | 339 | Glyceraldehyde-3-phosphate dehydrogenase | PRO_0000145669 | |||||
Regions | |||||||||
| Nucleotide binding | 12 – 13 | 2 | NAD By similarity | ||||||
| Region | 157 – 159 | 3 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
| Region | 216 – 217 | 2 | Glyceraldehyde 3-phosphate binding By similarity | ||||||
Sites | |||||||||
| Active site | 158 | 1 | Nucleophile By similarity | ||||||
| Binding site | 39 | 1 | NAD By similarity | ||||||
| Binding site | 84 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 188 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 203 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 239 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 320 | 1 | NAD By similarity | ||||||
| Site | 185 | 1 | Activates thiol group during catalysis By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Smith D.R., Robison K. Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. Barrell B.G.Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U00013 Genomic DNA. Translation: AAA17130.1. AL583919 Genomic DNA. Translation: CAC30078.1. |
| PIR | S72763. |
| RefSeq | NP_301482.1. NC_002677.1. |
3D structure databases | |
| ProteinModelPortal | P46713. |
| SMR | P46713. Positions 3-337. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000029430; EBMYCP00000029036; EBMYCG00000029425. |
| GeneID | 909341. |
| GenomeReviews | Gene locus ML0570 in contig AL450380_GR. |
| KEGG | mle:ML0570. |
| NMPDR | fig|272631.1.peg.354. |
| PATRIC | 18052102. VBIMycLep78757_0998. |
Organism-specific databases | |
| Leproma | ML0570. |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000017630. |
| HOGENOM | HBG571736. |
| OMA | PAKHTVI. |
| ProtClustDB | CLSK791163. |
Enzyme and pathway databases | |
| BioCyc | MLEP272631:ML0570-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 | G3P_MYCLE | ||||||||
| Accession | Primary (citable) accession number: P46713 | ||||||||
| 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 |

Clusters with