Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

gap

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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.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 (gap)
  2. Bifunctional PGK/TIM (pgk/tpi), Phosphoglycerate kinase (Tmari_0689)
  3. Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM)
  4. Enolase (eno), Enolase (eno)
  5. Pyruvate kinase (pyk), Pyruvate kinase (Tmari_0206)
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 – 351NAD1 Publication
Binding sitei121 – 1211NAD1 Publication
Active sitei152 – 1521NucleophileBy similarity
Sitei179 – 1791Activates thiol group during catalysisBy similarity
Binding sitei182 – 1821Glyceraldehyde 3-phosphate1 Publication
Binding sitei183 – 1831NAD1 Publication
Binding sitei197 – 1971Glyceraldehyde 3-phosphate1 Publication
Binding sitei233 – 2331Glyceraldehyde 3-phosphate1 Publication
Binding sitei315 – 3151NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 122NAD1 Publication

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

BioCyciMetaCyc:MONOMER-401.
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
Ordered Locus Names:TM_0688
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 333332Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145711Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi243274.TM0688.

Structurei

Secondary structure

1
333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi11 – 2313Combined sources
Beta strandi29 – 346Combined sources
Helixi39 – 479Combined sources
Turni50 – 523Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 686Combined sources
Beta strandi71 – 766Combined sources
Helixi81 – 833Combined sources
Helixi86 – 894Combined sources
Beta strandi93 – 964Combined sources
Beta strandi98 – 1003Combined sources
Helixi104 – 1074Combined sources
Helixi109 – 1124Combined sources
Beta strandi116 – 1227Combined sources
Beta strandi128 – 1303Combined sources
Turni133 – 1353Combined sources
Helixi137 – 1393Combined sources
Beta strandi146 – 1483Combined sources
Helixi152 – 16817Combined sources
Beta strandi170 – 18011Combined sources
Beta strandi185 – 1895Combined sources
Turni195 – 1984Combined sources
Helixi201 – 2033Combined sources
Beta strandi206 – 2083Combined sources
Helixi212 – 2198Combined sources
Helixi221 – 2233Combined sources
Turni224 – 2263Combined sources
Beta strandi227 – 2359Combined sources
Beta strandi240 – 25011Combined sources
Helixi254 – 26512Combined sources
Turni266 – 2727Combined sources
Beta strandi273 – 2764Combined sources
Helixi282 – 2854Combined sources
Beta strandi291 – 2955Combined sources
Turni296 – 2983Combined sources
Beta strandi300 – 3023Combined sources
Turni303 – 3053Combined sources
Beta strandi306 – 3138Combined sources
Helixi317 – 32913Combined sources
Helixi330 – 3323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HDGX-ray2.50O/Q2-333[»]
ProteinModelPortaliP17721.
SMRiP17721. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17721.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 1533Glyceraldehyde 3-phosphate binding1 Publication
Regioni210 – 2112Glyceraldehyde 3-phosphate binding1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C17. Bacteria.
COG0057. LUCA.
InParanoidiP17721.
KOiK00134.
OMAiFVRVLSW.
OrthoDBiEOG66TG3S.

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.

P17721-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARVAINGFG RIGRLVYRII YERKNPDIEV VAINDLTDTK TLAHLLKYDS
60 70 80 90 100
VHKKFPGKVE YTENSLIVDG KEIKVFAEPD PSKLPWKDLG VDFVIESTGV
110 120 130 140 150
FRNREKAELH LQAGAKKVII TAPAKGEDIT VVIGCNEDQL KPEHTIISCA
160 170 180 190 200
SCTTNSIAPI VKVLHEKFGI VSGMLTTVHS YTNDQRVLDL PHKDLRRARA
210 220 230 240 250
AAVNIIPTTT GAAKAVALVV PEVKGKLDGM AIRVPTPDGS ITDLTVLVEK
260 270 280 290 300
ETTVEEVNAV MKEATEGRLK GIIGYNDEPI VSSDIIGTTF SGIFDATITN
310 320 330
VIGGKLVKVA SWYDNEYGYS NRVVDTLELL LKM
Length:333
Mass (Da):36,425
Last modified:January 23, 2007 - v2
Checksum:i12B77104AB5E1CD0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72629 Genomic DNA. Translation: CAA51205.1.
AE000512 Genomic DNA. Translation: AAD35770.1.
PIRiS33325. DEHGGT.
RefSeqiNP_228497.1. NC_000853.1.
WP_004081074.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35770; AAD35770; TM_0688.
GeneIDi898355.
KEGGitma:TM0688.
PATRICi23936294. VBITheMar51294_0700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72629 Genomic DNA. Translation: CAA51205.1.
AE000512 Genomic DNA. Translation: AAD35770.1.
PIRiS33325. DEHGGT.
RefSeqiNP_228497.1. NC_000853.1.
WP_004081074.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HDGX-ray2.50O/Q2-333[»]
ProteinModelPortaliP17721.
SMRiP17721. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35770; AAD35770; TM_0688.
GeneIDi898355.
KEGGitma:TM0688.
PATRICi23936294. VBITheMar51294_0700.

Phylogenomic databases

eggNOGiENOG4105C17. Bacteria.
COG0057. LUCA.
InParanoidiP17721.
KOiK00134.
OMAiFVRVLSW.
OrthoDBiEOG66TG3S.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BioCyciMetaCyc:MONOMER-401.

Miscellaneous databases

EvolutionaryTraceiP17721.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Functional expression of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima in Escherichia coli. Authenticity and kinetic properties of the recombinant enzyme."
    Tomschy A., Glockhuber R., Jaenicke R.
    Eur. J. Biochem. 214:43-50(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  3. "Complete amino-acid sequence of glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima."
    Schultes V., Deutzmann R., Jaenicke R.
    Eur. J. Biochem. 192:25-31(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-333.
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  4. "The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5-A resolution."
    Korndoerfer I., Steipe B., Huber R., Tomschy A., Jaenicke R.
    J. Mol. Biol. 246:511-521(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

Entry informationi

Entry nameiG3P_THEMA
AccessioniPrimary (citable) accession number: P17721
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 141 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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.