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Protein

Putative glyceraldehyde-3-phosphate dehydrogenase C

Gene

gapC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein uncertaini

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. Putative glyceraldehyde-3-phosphate dehydrogenase C (gapC), Glyceraldehyde-3-phosphate dehydrogenase A (gapA)
  2. Phosphoglycerate kinase (pgk)
  3. Probable phosphoglycerate mutase GpmB (gpmB), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase I (pykF), Pyruvate kinase II (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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341NADBy similarity
Binding sitei78 – 781NADBy similarity
Binding sitei120 – 1201NADBy similarity
Active sitei150 – 1501NucleophileBy similarity
Sitei177 – 1771Activates thiol group during catalysisBy similarity
Binding sitei180 – 1801Glyceraldehyde 3-phosphateBy similarity
Binding sitei232 – 2321Glyceraldehyde 3-phosphateBy similarity
Binding sitei315 – 3151NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 122NADBy similarity

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

BioCyciEcoCyc:EG12103-MONOMER.
EcoCyc:G8205-MONOMER.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative glyceraldehyde-3-phosphate dehydrogenase C1 Publication (EC:1.2.1.12By similarity)
Short name:
GAPDH-C1 Publication
Alternative name(s):
NAD-dependent glyceraldehyde-3-phosphate dehydrogenase1 Publication
Gene namesi
Name:gapC1 Publication
Ordered Locus Names:b4493, JW1413/JW5906
ORF Names:b1416/b1417
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12103. gapC.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Putative glyceraldehyde-3-phosphate dehydrogenase CPRO_0000145649Add
BLAST

Proteomic databases

PRIDEiP33898.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

DIPiDIP-9737N.

Structurei

3D structure databases

ProteinModelPortaliP33898.
SMRiP33898. Positions 3-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 1513Glyceraldehyde 3-phosphate bindingBy similarity
Regioni209 – 2102Glyceraldehyde 3-phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000071678.
InParanoidiP33898.
PhylomeDBiP33898.

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.

P33898-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKVGINGFG RIGRLVLGRL LEVKSNIDVV AINDLTSPKI LAYLLKHDSN
60 70 80 90 100
YGPFPWSVDF TEDSLIVDGK SIAVYAEKEA KNIPWKAKGA EIIVECTGFY
110 120 130 140 150
TSAEKSQAHL DAGAKKVLIS APAGEMKTIV YNVNDDTLDG NDTIVSVASC
160 170 180 190 200
TTNCLAPMAK ALHDSFGIEV GTMTTIHAYT GTQSLVDGPR GKDLRASRAA
210 220 230 240 250
AENIIPHTTG AAKAIGLVIP ELSGKLKGHA QRVPVKTGSV TELVSILGKK
260 270 280 290 300
VTAEEVNNAL KQATTNNESF GYTDEEIVSS DIIGSHFGSV FDATQTEITA
310 320 330
VGDLQLVKTV AWYDNEYGFV TQLIRTLEKF AKL
Length:333
Mass (Da):35,650
Last modified:April 27, 2001 - v2
Checksum:iE88223297376B0A0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391K → Y (Ref. 8) Curated
Sequence conflicti39 – 391K → Y (PubMed:3780374).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS14477.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS14477.

3D structure databases

ProteinModelPortaliP33898.
SMRiP33898. Positions 3-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9737N.

Proteomic databases

PRIDEiP33898.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

EchoBASEiEB2027.
EcoGeneiEG12103. gapC.

Phylogenomic databases

HOGENOMiHOG000071678.
InParanoidiP33898.
PhylomeDBiP33898.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BioCyciEcoCyc:EG12103-MONOMER.
EcoCyc:G8205-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 nameiG3P2_ECOLI
AccessioniPrimary (citable) accession number: P33898
Secondary accession number(s): P76094
, P78062, P78291, Q03850, Q63208
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: April 27, 2001
Last modified: September 7, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.Curated
Ref. 8 and PubMed:3780374 sequences were originally thought to originate from rat.2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.