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Protein

Glyceraldehyde-3-phosphate dehydrogenase A

Gene

gapA

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.By similarity

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.By similarity

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.Curated
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase C (gapC), Glyceraldehyde-3-phosphate dehydrogenase A (gapA)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), Probable phosphoglycerate mutase GpmB (gpmB)
  4. Enolase (eno)
  5. Pyruvate kinase (ECs2564), Pyruvate kinase I (pykF), Pyruvate kinase (pykA)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei34NADBy similarity1
Binding sitei78NAD; via carbonyl oxygenBy similarity1
Binding sitei120NADBy similarity1
Active sitei150NucleophileBy similarity1
Sitei177Activates thiol group during catalysisBy similarity1
Binding sitei180Glyceraldehyde 3-phosphateBy similarity1
Binding sitei232Glyceraldehyde 3-phosphateBy similarity1
Binding sitei314NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 13NADBy similarity2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD, Nucleotide-binding

Enzyme and pathway databases

BioCyciECOO157:GAPA-MONOMER.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase ABy similarity (EC:1.2.1.12By similarity)
Short name:
GAPDH-ABy similarity
Alternative name(s):
NAD-dependent glyceraldehyde-3-phosphate dehydrogenaseBy similarity
Gene namesi
Name:gapA
Ordered Locus Names:Z2818, ECs2488
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001456512 – 331Glyceraldehyde-3-phosphate dehydrogenase AAdd BLAST330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei132N6-acetyllysineBy similarity1
Modified residuei138N6-acetyllysineBy similarity1
Modified residuei192N6-acetyllysineBy similarity1
Modified residuei249N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP0A9B4.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

MINTiMINT-1255388.
STRINGi155864.Z2818.

Structurei

3D structure databases

ProteinModelPortaliP0A9B4.
SMRiP0A9B4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni149 – 151Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni209 – 210Glyceraldehyde 3-phosphate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C17. Bacteria.
COG0057. LUCA.
HOGENOMiHOG000071678.
KOiK00134.
OMAiKWGEVGA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. 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]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A9B4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIKVGINGF GRIGRIVFRA AQKRSDIEIV AINDLLDADY MAYMLKYDST
60 70 80 90 100
HGRFDGTVEV KDGHLIVNGK KIRVTAERDP ANLKWDEVGV DVVAEATGLF
110 120 130 140 150
LTDETARKHI TAGAKKVVMT GPSKDNTPMF VKGANFDKYA GQDIVSNASC
160 170 180 190 200
TTNCLAPLAK VINDNFGIIE GLMTTVHATT ATQKTVDGPS HKDWRGGRGA
210 220 230 240 250
SQNIIPSSTG AAKAVGKVLP ELNGKLTGMA FRVPTPNVSV VDLTVRLEKA
260 270 280 290 300
ATYEQIKAAV KAAAEGEMKG VLGYTEDDVV STDFNGEVCT SVFDAKAGIA
310 320 330
LNDNFVKLVS WYDNETGYSN KVLDLIAHIS K
Length:331
Mass (Da):35,532
Last modified:January 23, 2007 - v2
Checksum:iB3A460AA6D59E46D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56768.1.
BA000007 Genomic DNA. Translation: BAB35911.1.
PIRiD85788.
H90939.
RefSeqiNP_310515.1. NC_002695.1.
WP_000153502.1. NZ_LPWC02000002.1.

Genome annotation databases

EnsemblBacteriaiAAG56768; AAG56768; Z2818.
BAB35911; BAB35911; BAB35911.
GeneIDi913285.
KEGGiece:Z2818.
ecs:ECs2488.
PATRICi18354332. VBIEscCol44059_2377.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56768.1.
BA000007 Genomic DNA. Translation: BAB35911.1.
PIRiD85788.
H90939.
RefSeqiNP_310515.1. NC_002695.1.
WP_000153502.1. NZ_LPWC02000002.1.

3D structure databases

ProteinModelPortaliP0A9B4.
SMRiP0A9B4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1255388.
STRINGi155864.Z2818.

Proteomic databases

PRIDEiP0A9B4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG56768; AAG56768; Z2818.
BAB35911; BAB35911; BAB35911.
GeneIDi913285.
KEGGiece:Z2818.
ecs:ECs2488.
PATRICi18354332. VBIEscCol44059_2377.

Phylogenomic databases

eggNOGiENOG4105C17. Bacteria.
COG0057. LUCA.
HOGENOMiHOG000071678.
KOiK00134.
OMAiKWGEVGA.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BioCyciECOO157:GAPA-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. 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]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiG3P1_ECO57
AccessioniPrimary (citable) accession number: P0A9B4
Secondary accession number(s): P06977
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.