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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene
N/A
Organism
Echinococcus multilocularis (Fox tapeworm)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (EmuJ_001101100), Glyceraldehyde-3-phosphate dehydrogenase (EmuJ_000254600), 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. Pyruvate kinase (EmuJ_001035200), Pyruvate kinase (EmuJ_001001900), Pyruvate kinase (EmuJ_001078100), Pyruvate kinase (EmuJ_000715400), Pyruvate kinase (EmuJ_001035400)
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 sitei34NADBy similarity1
Binding sitei79NAD; via carbonyl oxygenBy similarity1
Active sitei151NucleophilePROSITE-ProRule annotation1
Sitei178Activates thiol group during catalysisBy similarity1
Binding sitei181Glyceraldehyde 3-phosphateBy similarity1
Binding sitei233Glyceraldehyde 3-phosphateBy similarity1
Binding sitei316NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 13NADBy similarity2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.12)
Short name:
GAPDH
OrganismiEchinococcus multilocularis (Fox tapeworm)
Taxonomic identifieri6211 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesCestodaEucestodaCyclophyllideaTaeniidaeEchinococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001455151 – 336Glyceraldehyde-3-phosphate dehydrogenaseAdd BLAST336

Proteomic databases

PRIDEiQ27652.

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ27652.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni150 – 152Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni210 – 211Glyceraldehyde 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.

Q27652-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPQVGINGF GRIGRLVLRA AVASNSVNVV AVNDPFIDLE YMVYMFKYDS
60 70 80 90 100
AHGRYKGDVK VDGGKLVIDS HRITVFQEMS ASAVPWSQAG AEYIVESTGI
110 120 130 140 150
NTTVEKASAH FQGGAKKVII SAPSADSSHV RVGVNHEKYD PSMKVVSNAS
160 170 180 190 200
CTTNCLAPLA KVINDNFGIV EGLMTTVHSY TATQKVVDGP SKKAWRDGRT
210 220 230 240 250
AAQNIVPAST GAAKRVGKVI PELNGKLTGM AFRVPTPNVS VVDLTCKLSK
260 270 280 290 300
PATYDQIKAA VKRASESSAL KRILEYTEDQ VVSTDFLSTT CSSTFDARAG
310 320 330
IALNDTFVKL IAWYDNEFGY SCRVVDLISY MFKRDH
Length:336
Mass (Da):36,391
Last modified:November 1, 1996 - v1
Checksum:i2BED6F589C9984E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19101 mRNA. Translation: AAA61574.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19101 mRNA. Translation: AAA61574.1.

3D structure databases

ProteinModelPortaliQ27652.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ27652.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.

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_ECHMU
AccessioniPrimary (citable) accession number: Q27652
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.