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ECOLI:G3P1

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) gapA
Protein Name(s) Glyceraldehyde-3-phosphate dehydrogenase A

GAPDH-A

External Links
UniProt P0A9B2
EMBL X02662
U00096
AP009048
M66870
M66871
M66872
M66873
M66874
M66875
M66876
M66877
M66878
M66879
M66880
M66881
M66882
U07750
U07751
U07752
U07754
U07765
U07768
U07769
U07770
U07771
U07772
U07773
PIR A25209
RefSeq NP_416293.1
YP_490040.1
PDB 1DC3
1DC4
1DC5
1DC6
1GAD
1GAE
1S7C
2VYN
2VYV
PDBsum 1DC3
1DC4
1DC5
1DC6
1GAD
1GAE
1S7C
2VYN
2VYV
ProteinModelPortal P0A9B2
SMR P0A9B2
BioGrid 851992
DIP DIP-31848N
IntAct P0A9B2
MINT MINT-1255410
STRING 511145.b1779
SWISS-2DPAGE P0A9B2
PaxDb P0A9B2
PRIDE P0A9B2
EnsemblBacteria AAC74849
BAA15576
GeneID 12931314
947679
KEGG ecj:Y75_p1754
eco:b1779
PATRIC 32118869
EchoBASE EB0362
EcoGene EG10367
eggNOG COG0057
HOGENOM HOG000071678
InParanoid P0A9B2
KO K00134
OMA YKGEAII
OrthoDB EOG66TG3S
PhylomeDB P0A9B2
BioCyc EcoCyc:GAPDH-A-MONOMER
ECOL316407:JW1768-MONOMER
MetaCyc:GAPDH-A-MONOMER
SABIO-RK P0A9B2
UniPathway UPA00109
EvolutionaryTrace P0A9B2
PRO PR:P0A9B2
Proteomes UP000000318
UP000000625
Genevestigator P0A9B2
GO GO:0005829
GO:0016020
GO:0004365
GO:0051287
GO:0050661
GO:0006006
GO:0006096
Gene3D 3.40.50.720
InterPro IPR020831
IPR020830
IPR020829
IPR020828
IPR006424
IPR016040
PANTHER PTHR10836
Pfam PF02800
PF00044
PIRSF PIRSF000149
PRINTS PR00078
SMART SM00846
TIGRFAMs TIGR01534
PROSITE PS00071

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004365

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

PMID:9260967[1]

ECO:0000315

F

Table 3. When a phage is inserted into gapA no cell growth is detected, due to the lack of GAPDHase activity.

complete

GO:0006096

glycolysis

PMID:9260967[1]

ECO:0000315

P

Table 3. When a phage was inserted into gapA the E. coli strain was inable to grow on glucose. Expression of gapA completely restored this ability confirming it's role in glycolysis.

complete

enables

GO:0051287

NAD binding

PMID:19542219[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004365

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity

PMID:2659073[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:16858726[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10367
FB:FBgn0001091
FB:FBgn0001092
MGI:MGI:95653
PANTHER:PTN000089473
RGD:2661
SGD:S000003424
SGD:S000003588
SGD:S000003769
TAIR:locus:2103085

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10367
MGI:MGI:95640
PANTHER:PTN000089473
RGD:2661
SGD:S000003424
SGD:S000003588
SGD:S000003769
TAIR:locus:2103085
UniProtKB:M0R590
UniProtKB:P04406
UniProtKB:Q8IKK7
UniProtKB:Q9FX54

C

Seeded From UniProt

complete

enables

GO:0004365

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10367
FB:FBgn0001091
FB:FBgn0001092
MGI:MGI:95640
MGI:MGI:95653
PANTHER:PTN000089473
RGD:2661
SGD:S000003424
SGD:S000003588
SGD:S000003769
TAIR:locus:2032810
TAIR:locus:2206435
UniProtKB:M0R590
UniProtKB:O14556
UniProtKB:P04406
UniProtKB:P20445
UniProtKB:Q9FX54

F

Seeded From UniProt

complete

enables

GO:0051287

NAD binding

PMID:10190977[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9B2

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:9260967[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:17309111[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004365

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity

PMID:10190977[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006006

glucose metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006424

P

Seeded From UniProt

complete

enables

GO:0016620

oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006424
InterPro:IPR020828
InterPro:IPR020829
InterPro:IPR020830
InterPro:IPR020831

F

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006424

F

Seeded From UniProt

complete

enables

GO:0051287

NAD binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006424

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006424
InterPro:IPR020828
InterPro:IPR020829
InterPro:IPR020830
InterPro:IPR020831

P

Seeded From UniProt

complete

enables

GO:0004365

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.2.1.12

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0324
UniPathway:UPA00109

P

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 Seta, FD et al. (1997) Characterization of Escherichia coli strains with gapA and gapB genes deleted. J. Bacteriol. 179 5218-21 PubMed GONUTS page
  2. ↑ Frayne, J et al. (2009) Structure of insoluble rat sperm glyceraldehyde-3-phosphate dehydrogenase (GAPDH) via heterotetramer formation with Escherichia coli GAPDH reveals target for contraceptive design. J. Biol. Chem. 284 22703-12 PubMed GONUTS page
  3. ↑ Soukri, A et al. (1989) Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis. Biochemistry 28 2586-92 PubMed GONUTS page
  4. ↑ 4.0 4.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  6. ↑ 6.0 6.1 Eyschen, J et al. (1999) Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ nicotinamide but does not experience A-specific hydride transfer. Arch. Biochem. Biophys. 364 219-27 PubMed GONUTS page
  7. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  8. ↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
  9. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
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