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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

gap

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.2 Publications

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 (gap)
  2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI_1)
  4. Enolase (eno), Enolase (eno), Enolase (eno)
  5. Pyruvate kinase (pyk), Pyruvate kinase (AA904_05055), Pyruvate kinase (pyk), Pyruvate kinase (GT94_09925), Pyruvate kinase (B4114_2369)
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 sitei34NAD4 Publications1
Binding sitei78NAD; via carbonyl oxygen4 Publications1
Binding sitei120NAD4 Publications1
Active sitei152Nucleophile1 Publication1 Publication1
Sitei179Activates thiol group during catalysisBy similarity1
Binding sitei182Glyceraldehyde 3-phosphate5 Publications1
Binding sitei183NAD4 Publications1
Binding sitei197Glyceraldehyde 3-phosphate3 Publications1
Binding sitei233Glyceraldehyde 3-phosphate5 Publications1
Binding sitei315NAD4 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 13NAD4 Publications2

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

BRENDAi1.2.1.12. 623.
SABIO-RKP00362.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase1 Publication (EC:1.2.1.12By similarity)
Short name:
GAPDH1 Publication
Alternative name(s):
NAD-dependent glyceraldehyde-3-phosphate dehydrogenase1 Publication
Gene namesi
Name:gap
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi35 – 37LTD → TGG in mutant B-S, the recognition of NAD is slightly affected; when associated with A-190 and S-191. 1 Publication3
Mutagenesisi152C → A: Loss of dehydrogenase activity. 2 Publications1
Mutagenesisi152C → S: Possess a low residual dehydrogenase activity. 1 Publication1
Mutagenesisi190L → A in mutant D32G-S, a strong alteration of the affinity for NAD is observed; when associated with S-191. In mutant B-S, the recognition of NAD is slightly affected; when associated with 35-T--G-37 and S-191. 1 Publication1
Mutagenesisi191P → S in mutant D32G-S, a strong alteration of the affinity for NAD is observed; when associated with A-190. In mutant B-S, the recognition of NAD is slightly affected; when associated with 35-T--G-37 and A-190. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001456332 – 335Glyceraldehyde-3-phosphate dehydrogenaseAdd BLAST334

Proteomic databases

PRIDEiP00362.

Interactioni

Subunit structurei

Homotetramer.6 Publications

Structurei

Secondary structure

1335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi12 – 21Combined sources10
Beta strandi27 – 33Combined sources7
Helixi38 – 46Combined sources9
Turni49 – 51Combined sources3
Beta strandi58 – 61Combined sources4
Beta strandi64 – 67Combined sources4
Beta strandi70 – 75Combined sources6
Helixi80 – 82Combined sources3
Helixi86 – 88Combined sources3
Beta strandi92 – 95Combined sources4
Beta strandi97 – 99Combined sources3
Helixi103 – 106Combined sources4
Helixi108 – 111Combined sources4
Beta strandi115 – 121Combined sources7
Beta strandi127 – 129Combined sources3
Turni132 – 134Combined sources3
Helixi136 – 138Combined sources3
Turni141 – 143Combined sources3
Beta strandi146 – 148Combined sources3
Helixi152 – 168Combined sources17
Beta strandi170 – 180Combined sources11
Beta strandi185 – 189Combined sources5
Turni195 – 198Combined sources4
Turni201 – 203Combined sources3
Beta strandi206 – 209Combined sources4
Helixi212 – 219Combined sources8
Helixi221 – 223Combined sources3
Turni224 – 226Combined sources3
Beta strandi227 – 235Combined sources9
Beta strandi240 – 250Combined sources11
Helixi254 – 266Combined sources13
Turni267 – 272Combined sources6
Beta strandi273 – 276Combined sources4
Helixi282 – 285Combined sources4
Beta strandi290 – 295Combined sources6
Helixi296 – 298Combined sources3
Beta strandi300 – 302Combined sources3
Turni303 – 305Combined sources3
Beta strandi306 – 313Combined sources8
Helixi317 – 332Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DBVX-ray2.50O/P/Q/R2-335[»]
1GD1X-ray1.80O/P/Q/R2-335[»]
1NPTX-ray2.18O/P/Q/R2-335[»]
1NQ5X-ray2.11A/C/O/Q2-335[»]
1NQAX-ray2.20O/P/Q/R2-335[»]
1NQOX-ray2.01A/C/O/Q2-335[»]
2DBVX-ray2.20O/P/Q/R2-335[»]
2GD1X-ray2.50O/P/Q/R2-335[»]
3CMCX-ray1.77O/P/Q/R2-335[»]
3DBVX-ray2.45O/P/Q/R2-335[»]
4DBVX-ray2.50O/P/Q/R2-335[»]
ProteinModelPortaliP00362.
SMRiP00362.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00362.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni151 – 153Glyceraldehyde 3-phosphate binding5 Publications3
Regioni210 – 211Glyceraldehyde 3-phosphate binding4 Publications2

Sequence similaritiesi

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.

P00362-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVKVGINGF GRIGRNVFRA ALKNPDIEVV AVNDLTDANT LAHLLKYDSV
60 70 80 90 100
HGRLDAEVSV NGNNLVVNGK EIIVKAERDP ENLAWGEIGV DIVVESTGRF
110 120 130 140 150
TKREDAAKHL EAGAKKVIIS APAKNEDITI VMGVNQDKYD PKAHHVISNA
160 170 180 190 200
SCTTNCLAPF AKVLHEQFGI VRGMMTTVHS YTNDQRILDL PHKDLRRARA
210 220 230 240 250
AAESIIPTTT GAAKAVALVL PELKGKLNGM AMRVPTPNVS VVDLVAELEK
260 270 280 290 300
EVTVEEVNAA LKAAAEGELK GILAYSEEPL VSRDYNGSTV SSTIDALSTM
310 320 330
VIDGKMVKVV SWYDNETGYS HRVVDLAAYI ASKGL
Length:335
Mass (Da):36,075
Last modified:January 23, 2007 - v5
Checksum:iDBAAA2DD24497E18
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24493 Genomic DNA. Translation: AAA22461.1.
PIRiJS0164. DEBSGF.
RefSeqiWP_033015082.1. NZ_LUCR01000219.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24493 Genomic DNA. Translation: AAA22461.1.
PIRiJS0164. DEBSGF.
RefSeqiWP_033015082.1. NZ_LUCR01000219.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DBVX-ray2.50O/P/Q/R2-335[»]
1GD1X-ray1.80O/P/Q/R2-335[»]
1NPTX-ray2.18O/P/Q/R2-335[»]
1NQ5X-ray2.11A/C/O/Q2-335[»]
1NQAX-ray2.20O/P/Q/R2-335[»]
1NQOX-ray2.01A/C/O/Q2-335[»]
2DBVX-ray2.20O/P/Q/R2-335[»]
2GD1X-ray2.50O/P/Q/R2-335[»]
3CMCX-ray1.77O/P/Q/R2-335[»]
3DBVX-ray2.45O/P/Q/R2-335[»]
4DBVX-ray2.50O/P/Q/R2-335[»]
ProteinModelPortaliP00362.
SMRiP00362.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP00362.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BRENDAi1.2.1.12. 623.
SABIO-RKP00362.

Miscellaneous databases

EvolutionaryTraceiP00362.

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 nameiG3P_GEOSE
AccessioniPrimary (citable) accession number: P00362
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 133 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

PubMed:2684782 sequence was incorrect and retracted in PubMed:2227448.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.