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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391NAD2 Publications
Binding sitei92 – 921NAD; via carbonyl oxygen2 Publications
Binding sitei135 – 1351NAD2 Publications
Active sitei167 – 1671Nucleophile
Sitei195 – 1951Activates thiol group during catalysis
Binding sitei198 – 1981Glyceraldehyde 3-phosphateBy similarity
Binding sitei250 – 2501Glyceraldehyde 3-phosphateBy similarity
Binding sitei336 – 3361NAD2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 142NAD2 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 361360Glyceraldehyde-3-phosphate dehydrogenase, glycosomalPRO_0000145529Add
BLAST

Proteomic databases

PRIDEiQ27890.

Interactioni

Subunit structurei

Homotetramer.4 Publications

Structurei

Secondary structure

1
361
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi13 – 2412Combined sources
Turni29 – 313Combined sources
Beta strandi32 – 409Combined sources
Helixi44 – 529Combined sources
Turni55 – 573Combined sources
Beta strandi64 – 674Combined sources
Beta strandi73 – 753Combined sources
Beta strandi78 – 814Combined sources
Beta strandi84 – 907Combined sources
Helixi95 – 973Combined sources
Helixi100 – 1034Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi112 – 1143Combined sources
Helixi118 – 1214Combined sources
Helixi123 – 1264Combined sources
Beta strandi130 – 1367Combined sources
Beta strandi139 – 1413Combined sources
Turni147 – 1493Combined sources
Helixi151 – 1533Combined sources
Turni156 – 1583Combined sources
Beta strandi160 – 1634Combined sources
Helixi167 – 18115Combined sources
Beta strandi189 – 1968Combined sources
Beta strandi201 – 2055Combined sources
Beta strandi209 – 2124Combined sources
Helixi213 – 2153Combined sources
Helixi218 – 2203Combined sources
Beta strandi223 – 2264Combined sources
Helixi229 – 2368Combined sources
Helixi238 – 2403Combined sources
Turni241 – 2433Combined sources
Beta strandi244 – 2529Combined sources
Beta strandi257 – 2648Combined sources
Helixi271 – 28313Combined sources
Turni284 – 2896Combined sources
Beta strandi290 – 2934Combined sources
Helixi299 – 3024Combined sources
Beta strandi308 – 3125Combined sources
Helixi313 – 3186Combined sources
Beta strandi325 – 33410Combined sources
Helixi338 – 35720Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ27890.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 1683Glyceraldehyde 3-phosphate bindingBy similarity
Regioni227 – 2282Glyceraldehyde 3-phosphate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi359 – 3613Microbody targeting signalSequence analysis

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
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. Positions 2-359.
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: December 9, 2015
This is version 108 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.