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Protein

Glyceraldehyde-3-phosphate dehydrogenase, glycosomal

Gene

GAPG

Organism
Leishmania mexicana
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, cytosolic (GAPC), Glyceraldehyde-3-phosphate dehydrogenase, glycosomal (GAPG)
  2. Phosphoglycerate kinase, cytosolic (PGKB), Phosphoglycerate kinase, glycosomal (PGKC)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. Pyruvate kinase (PYK)
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 sitei39NAD2 Publications1
Binding sitei92NAD; via carbonyl oxygen2 Publications1
Binding sitei135NAD2 Publications1
Active sitei167Nucleophile1
Sitei195Activates thiol group during catalysis1
Binding sitei198Glyceraldehyde 3-phosphateBy similarity1
Binding sitei250Glyceraldehyde 3-phosphateBy similarity1
Binding sitei336NAD2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 14NAD2 Publications2

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. 2951.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase, glycosomal (EC:1.2.1.12)
Short name:
GAPDH
Gene namesi
Name:GAPG
OrganismiLeishmania mexicana
Taxonomic identifieri5665 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Glycosome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001455292 – 361Glyceraldehyde-3-phosphate dehydrogenase, glycosomalAdd BLAST360

Proteomic databases

PRIDEiQ27890.

Interactioni

Subunit structurei

Homotetramer.4 Publications

Structurei

Secondary structure

1361
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi13 – 24Combined sources12
Turni29 – 31Combined sources3
Beta strandi32 – 40Combined sources9
Helixi44 – 52Combined sources9
Turni55 – 57Combined sources3
Beta strandi64 – 67Combined sources4
Beta strandi73 – 75Combined sources3
Beta strandi78 – 81Combined sources4
Beta strandi84 – 90Combined sources7
Helixi95 – 97Combined sources3
Helixi100 – 103Combined sources4
Beta strandi107 – 110Combined sources4
Beta strandi112 – 114Combined sources3
Helixi118 – 121Combined sources4
Helixi123 – 126Combined sources4
Beta strandi130 – 136Combined sources7
Beta strandi139 – 141Combined sources3
Turni147 – 149Combined sources3
Helixi151 – 153Combined sources3
Turni156 – 158Combined sources3
Beta strandi160 – 163Combined sources4
Helixi167 – 181Combined sources15
Beta strandi189 – 196Combined sources8
Beta strandi201 – 205Combined sources5
Beta strandi209 – 212Combined sources4
Helixi213 – 215Combined sources3
Helixi218 – 220Combined sources3
Beta strandi223 – 226Combined sources4
Helixi229 – 236Combined sources8
Helixi238 – 240Combined sources3
Turni241 – 243Combined sources3
Beta strandi244 – 252Combined sources9
Beta strandi257 – 264Combined sources8
Helixi271 – 283Combined sources13
Turni284 – 289Combined sources6
Beta strandi290 – 293Combined sources4
Helixi299 – 302Combined sources4
Beta strandi308 – 312Combined sources5
Helixi313 – 318Combined sources6
Beta strandi325 – 334Combined sources10
Helixi338 – 357Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A7KX-ray2.80A/B/C/D2-361[»]
1GYPX-ray2.80A/B/C/D2-359[»]
1GYQX-ray3.40A/B/C/D2-359[»]
1I32X-ray2.60A/B/C/D/E/F2-361[»]
1I33X-ray3.00A/B/C/D/E/F2-361[»]
ProteinModelPortaliQ27890.
SMRiQ27890.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ27890.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni166 – 168Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni227 – 228Glyceraldehyde 3-phosphate bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi359 – 361Microbody targeting signalSequence analysis3

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.

Q27890-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPIKVGING FGRIGRMVFQ AICDQGLIGT EIDVVAVVDM STNAEYFAYQ
60 70 80 90 100
MKHDTVHGRP KYTVEAVKSS PSVETADVLV VNGHRIKCVK AQRNPADLPW
110 120 130 140 150
GKLGVDYVIE STGLFTDKLK AEGHIKGGAK KVVISAPASG GAKTIVMGVN
160 170 180 190 200
QHEYSPASHH VVSNASCTTN CLAPIVHVLT KENFGIETGL MTTIHSYTAT
210 220 230 240 250
QKTVDGVSLK DWRGGRAAAV NIIPSTTGAA KAVGMVIPST KGKLTGMSFR
260 270 280 290 300
VPTPDVSVVD LTFRATRDTS IQEIDKAIKK AAQTYMKGIL GFTDEELVSA
310 320 330 340 350
DFINDNRSSV YDSKATLQNN LPGEKRFFKV VSWYDNEWAY SHRVVDLVRY
360
MAAKDAASSK M
Length:361
Mass (Da):39,033
Last modified:January 23, 2007 - v3
Checksum:i01B116A02CD7D3B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65226 Genomic DNA. Translation: CAA46334.1.
X65226 Genomic DNA. Translation: CAA46333.1.
PIRiA48445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65226 Genomic DNA. Translation: CAA46334.1.
X65226 Genomic DNA. Translation: CAA46333.1.
PIRiA48445.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A7KX-ray2.80A/B/C/D2-361[»]
1GYPX-ray2.80A/B/C/D2-359[»]
1GYQX-ray3.40A/B/C/D2-359[»]
1I32X-ray2.60A/B/C/D/E/F2-361[»]
1I33X-ray3.00A/B/C/D/E/F2-361[»]
ProteinModelPortaliQ27890.
SMRiQ27890.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ27890.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BRENDAi1.2.1.12. 2951.

Miscellaneous databases

EvolutionaryTraceiQ27890.

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 nameiG3PG_LEIME
AccessioniPrimary (citable) accession number: Q27890
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 110 of the entry and version 3 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.