Reviewed,
UniProtKB/Swiss-Prot P33898 (G3P3_ECOLI)
Last modified
June 16, 2009.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative glyceraldehyde-3-phosphate dehydrogenase C Short name=GAPDH-C EC=1.2.1.12 | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 333 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Uncertain. |
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 | Cytoplasm Potential. |
| Sequence similarities | Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. |
| Caution | Could be the product of a pseudogene; in K12 this gene is disrupted by a stop codon and a frameshift. It seems to be intact in a number of wild-type strains. Ref.8 and Ref.9 sequences were originally thought to originate from rat. |
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 oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (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 – 333 | 333 | Putative glyceraldehyde-3-phosphate dehydrogenase C | PRO_0000145649 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 12 | 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 | 315 | 1 | NAD By similarity | ||||||
| Site | 177 | 1 | Activates thiol group during catalysis By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 39 | 1 | K → Y Ref.8 | ||||||
| Sequence conflict | 39 | 1 | K → Y Ref.9 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A second Escherichia coli gene with similarity to gapA." Hidalgo E., Limon A., Aguilar J. Microbiologia 12:99-106(1996) [PubMed: 9019141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [2] | "Escherichia coli genes expressed preferentially in an aquatic environment." Espinosa-Urgel M., Kolter R. Mol. Microbiol. 28:325-332(1998) [PubMed: 9622357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Clinical isolate and River isolate. |
| [3] | "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T.DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [5] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [6] | "Molecular cloning and DNA sequencing of the Escherichia coli K-12 ald gene encoding aldehyde dehydrogenase." Hidalgo E., Chen Y.-M., Lin E.C.C., Aguilar J. J. Bacteriol. 173:6118-6123(1991) [PubMed: 1917845] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 306-332. Strain: K12. |
| [7] | "Nucleotide sequence of the cybB gene encoding cytochrome b561 in Escherichia coli K12." Nakamura H., Murakami H., Yamato I., Anraku Y. Mol. Gen. Genet. 212:1-5(1988) [PubMed: 2836696] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13. Strain: K12. |
| [8] | Krawetz S.A. Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-165. |
| [9] | "A vector-primer-cloner-sequencer plasmid for the construction of cDNA libraries: evidence for a rat glyceraldehyde-3-phosphate dehydrogenase-like mRNA and a ferritin mRNA within testis." Krawetz S.A., Connor W., Cannon P.D., Dixon G.H. DNA 5:427-435(1986) [PubMed: 3780374] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-52. |
Cross-references
Sequence databases | |
|---|---|
| L09067 Genomic DNA. Translation: AAA23856.1. Sequence problems. U00096 Genomic DNA. No translation available. AP009048 Genomic DNA. No translation available. M64541 Genomic DNA. No translation available. X07569 Genomic DNA. No translation available. X54798 mRNA. Translation: CAA38569.1. M14166 mRNA. Translation: AAA41178.1. | |
| PIR | S14477. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HDG based on UniProtKB P17721. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:9737N. |
Genome annotation databases | |
| GenomeReviews | Gene locus b4493 in contig AP009048_GR. |
Organism-specific databases | |
| EchoBASE | EB2027. |
| EcoGene | EG12103. gapC. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P33898. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:EG12103-MON. EcoCyc:G8205-MON. |
Family and domain databases | |
| InterPro | IPR000173. GlycerAld_3-P_DH. IPR006424. Glyceraldehyde-3-P_DH_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 | G3P3_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P33898 Secondary accession number(s): P76094 Q63208 | ||||||||
| 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
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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