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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

gap

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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

Enzyme regulationi

Resistant to pentalenolactone.

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 (gap)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase 2 (eno2), Enolase 1 (eno1)
  5. Pyruvate kinase (SCO5423), Pyruvate kinase (SCO2014)
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 sitei35 – 351NADBy similarity
Binding sitei79 – 791NAD; via carbonyl oxygenBy similarity
Binding sitei121 – 1211NADBy similarity
Active sitei153 – 1531NucleophileBy similarity
Sitei180 – 1801Activates thiol group during catalysisBy similarity
Binding sitei183 – 1831Glyceraldehyde 3-phosphateBy similarity
Binding sitei184 – 1841NADBy similarity
Binding sitei198 – 1981Glyceraldehyde 3-phosphateBy similarity
Binding sitei234 – 2341Glyceraldehyde 3-phosphateBy similarity
Binding sitei317 – 3171NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 132NADBy 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

UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenaseBy similarity (EC:1.2.1.12By similarity)
Short name:
GAPDHBy similarity
Alternative name(s):
NAD-dependent glyceraldehyde-3-phosphate dehydrogenaseBy similarity
Gene namesi
Name:gap
Ordered Locus Names:SCO1947
ORF Names:SCC54.07c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145701Add
BLAST

Proteomic databases

PRIDEiQ9Z518.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi100226.SCO1947.

Structurei

3D structure databases

ProteinModelPortaliQ9Z518.
SMRiQ9Z518. Positions 3-335.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni152 – 1543Glyceraldehyde 3-phosphate bindingBy similarity
Regioni211 – 2122Glyceraldehyde 3-phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C17. Bacteria.
COG0057. LUCA.
HOGENOMiHOG000071679.
InParanoidiQ9Z518.
KOiK00134.
OMAiFVRVLSW.
OrthoDBiPOG091H02BL.
PhylomeDBiQ9Z518.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. GlycerAld/Erythrose_P_DH.
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.

Sequencei

Sequence statusi: Complete.

Q9Z518-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIRVGINGF GRIGRNYFRA LLEQGADIEI VAVNDLGDTA TTAHLLKYDT
60 70 80 90 100
ILGRLKAEVS HTEDTITVDG KTIKVLSERN PADIPWGELG VDIVIESTGI
110 120 130 140 150
FTKKADAEKH IAGGAKKVLI SAPAKDEDIT IVMGVNQDKY DPANHHVISN
160 170 180 190 200
ASCTTNCVAP MAKVLDENFG IVKGLMTTVH AYTNDQRILD FPHKDLRRAR
210 220 230 240 250
AAAENIIPTT TGAAKATALV LPQLKGKLDG IAMRVPVPTG SATDLVVELQ
260 270 280 290 300
REVTKDEVNA AFKKAADDGD LKGILFYTED AIVSSDITGD PASCTFDSSL
310 320 330
TMVQEGKSVK ILGWYDNEWG YSNRLVDLTV FVGNQL
Length:336
Mass (Da):36,268
Last modified:May 1, 1999 - v1
Checksum:i91C17A1EB1EE3C18
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939110 Genomic DNA. Translation: CAB38137.1.
PIRiT36020.
RefSeqiNP_626211.1. NC_003888.3.
WP_003976871.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB38137; CAB38137; CAB38137.
GeneIDi1097381.
KEGGisco:SCO1947.
PATRICi23733528. VBIStrCoe124346_1974.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939110 Genomic DNA. Translation: CAB38137.1.
PIRiT36020.
RefSeqiNP_626211.1. NC_003888.3.
WP_003976871.1. NC_003888.3.

3D structure databases

ProteinModelPortaliQ9Z518.
SMRiQ9Z518. Positions 3-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO1947.

Proteomic databases

PRIDEiQ9Z518.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB38137; CAB38137; CAB38137.
GeneIDi1097381.
KEGGisco:SCO1947.
PATRICi23733528. VBIStrCoe124346_1974.

Phylogenomic databases

eggNOGiENOG4105C17. Bacteria.
COG0057. LUCA.
HOGENOMiHOG000071679.
InParanoidiQ9Z518.
KOiK00134.
OMAiFVRVLSW.
OrthoDBiPOG091H02BL.
PhylomeDBiQ9Z518.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. GlycerAld/Erythrose_P_DH.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiG3P_STRCO
AccessioniPrimary (citable) accession number: Q9Z518
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1999
Last modified: September 7, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.