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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene
N/A
Organism
Panulirus versicolor (Painted spiny lobster) (Palinurus versicolor)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.PROSITE-ProRule annotation

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
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 sitei31NAD1 Publication1
Binding sitei76NAD; via carbonyl oxygenBy similarity1
Active sitei148Nucleophile1
Sitei175Activates thiol group during catalysis1
Binding sitei178Glyceraldehyde 3-phosphateBy similarity1
Binding sitei230Glyceraldehyde 3-phosphateBy similarity1
Binding sitei312NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 11NAD1 Publication2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.12. 4494.
SABIO-RKP56649.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.12)
Short name:
GAPDH
OrganismiPanulirus versicolor (Painted spiny lobster) (Palinurus versicolor)
Taxonomic identifieri150436 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAchelataPalinuroideaPalinuridaePanulirus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001455061 – 333Glyceraldehyde-3-phosphate dehydrogenaseAdd BLAST333

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylserineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP56649.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Helixi10 – 22Combined sources13
Beta strandi26 – 30Combined sources5
Beta strandi32 – 34Combined sources3
Helixi36 – 44Combined sources9
Turni47 – 49Combined sources3
Beta strandi56 – 59Combined sources4
Beta strandi62 – 65Combined sources4
Beta strandi68 – 73Combined sources6
Helixi78 – 80Combined sources3
Helixi83 – 86Combined sources4
Beta strandi90 – 93Combined sources4
Beta strandi95 – 97Combined sources3
Helixi101 – 104Combined sources4
Helixi105 – 108Combined sources4
Turni109 – 111Combined sources3
Beta strandi113 – 119Combined sources7
Beta strandi122 – 124Combined sources3
Turni129 – 131Combined sources3
Helixi133 – 135Combined sources3
Beta strandi142 – 144Combined sources3
Helixi148 – 164Combined sources17
Beta strandi166 – 175Combined sources10
Beta strandi181 – 185Combined sources5
Helixi193 – 195Combined sources3
Turni198 – 200Combined sources3
Beta strandi203 – 205Combined sources3
Helixi209 – 216Combined sources8
Helixi218 – 220Combined sources3
Turni221 – 223Combined sources3
Beta strandi224 – 230Combined sources7
Beta strandi237 – 247Combined sources11
Helixi251 – 263Combined sources13
Turni264 – 269Combined sources6
Beta strandi270 – 273Combined sources4
Helixi279 – 282Combined sources4
Beta strandi288 – 292Combined sources5
Turni293 – 295Combined sources3
Beta strandi297 – 300Combined sources4
Beta strandi303 – 310Combined sources8
Helixi314 – 331Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CRWX-ray2.00G/R1-333[»]
1DSSX-ray1.88G/R1-333[»]
1IHXX-ray2.80A/B/C/D1-333[»]
1IHYX-ray3.00A/B/C/D1-333[»]
1SZJX-ray2.00G/R1-333[»]
ProteinModelPortaliP56649.
SMRiP56649.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56649.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni147 – 149Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni207 – 208Glyceraldehyde 3-phosphate bindingBy similarity2

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.

P56649-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SKIGINGFGR IGRLVLRAAL EMGAQVVAVN DPFIALEYMV YMFKYDSTHG
60 70 80 90 100
MFKGEVKAED GALVVDGKKI TVFNEMKPEN IPWSKAGAEY IVESTGVFTT
110 120 130 140 150
IEKASAHFKG GAKKVIISAP SADAPMFVCG VNLEKYSKDM KVVSNASCTT
160 170 180 190 200
NCLAPVAKVL HENFEIVEGL MTTVHAVTAT QKTVDGPSAK DWRGGRGAAQ
210 220 230 240 250
NIIPSSTGAA KAVGKVIPEL DGKLTGMAFR VPTPNVSVVD LTVRLGKECS
260 270 280 290 300
YDDIKAAMKA ASEGPLQGVL GYTEDDVVSC DFTGDNRSSI FDAKAGIQLS
310 320 330
KTFVKVVSWY DNEFGYSQRV IDLIKHMQKV DSA
Length:333
Mass (Da):35,724
Last modified:July 15, 1999 - v1
Checksum:i818572106E294C19
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CRWX-ray2.00G/R1-333[»]
1DSSX-ray1.88G/R1-333[»]
1IHXX-ray2.80A/B/C/D1-333[»]
1IHYX-ray3.00A/B/C/D1-333[»]
1SZJX-ray2.00G/R1-333[»]
ProteinModelPortaliP56649.
SMRiP56649.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP56649.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BRENDAi1.2.1.12. 4494.
SABIO-RKP56649.

Miscellaneous databases

EvolutionaryTraceiP56649.

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_PANVR
AccessioniPrimary (citable) accession number: P56649
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: November 2, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

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.