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Q27890 (G3PG_LEIME) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glyceraldehyde-3-phosphate dehydrogenase, glycosomal
Short name=GAPDH
EC=1.2.1.12
Gene names
Name:GAPG
OrganismLeishmania mexicana
Taxonomic identifier5665 [NCBI]
Taxonomic lineageEukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmania

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.

Subunit structure

Homotetramer. Ref.2 Ref.3 Ref.5

Subcellular location

Glycosome.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentGlycosome
Peroxisome
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentglycosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

NADP binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 361360Glyceraldehyde-3-phosphate dehydrogenase, glycosomal
PRO_0000145529

Regions

Nucleotide binding13 – 142NAD
Region166 – 1683Glyceraldehyde 3-phosphate binding By similarity
Region227 – 2282Glyceraldehyde 3-phosphate binding By similarity
Motif359 – 3613Microbody targeting signal Potential

Sites

Active site1671Nucleophile
Binding site391NAD
Binding site921NAD; via carbonyl oxygen
Binding site1351NAD
Binding site1981Glyceraldehyde 3-phosphate By similarity
Binding site2501Glyceraldehyde 3-phosphate By similarity
Binding site3361NAD
Site1951Activates thiol group during catalysis

Secondary structure

1 .......................................................................... 361
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q27890 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 01B116A02CD7D3B5

FASTA36139,033
        10         20         30         40         50         60 
MAPIKVGING FGRIGRMVFQ AICDQGLIGT EIDVVAVVDM STNAEYFAYQ MKHDTVHGRP 

        70         80         90        100        110        120 
KYTVEAVKSS PSVETADVLV VNGHRIKCVK AQRNPADLPW GKLGVDYVIE STGLFTDKLK 

       130        140        150        160        170        180 
AEGHIKGGAK KVVISAPASG GAKTIVMGVN QHEYSPASHH VVSNASCTTN CLAPIVHVLT 

       190        200        210        220        230        240 
KENFGIETGL MTTIHSYTAT QKTVDGVSLK DWRGGRAAAV NIIPSTTGAA KAVGMVIPST 

       250        260        270        280        290        300 
KGKLTGMSFR VPTPDVSVVD LTFRATRDTS IQEIDKAIKK AAQTYMKGIL GFTDEELVSA 

       310        320        330        340        350        360 
DFINDNRSSV YDSKATLQNN LPGEKRFFKV VSWYDNEWAY SHRVVDLVRY MAAKDAASSK 


M

« Hide

References

[1]"Molecular analysis of the cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase in Leishmania mexicana."
Hannaert V., Blaauw M., Kohl L., Allert S., Opperdoes F.R., Michels P.A.M.
Mol. Biochem. Parasitol. 55:115-126(1992) [PubMed: 1435864] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Crystal structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Leishmania mexicana: implications for structure-based drug design and a new position for the inorganic phosphate binding site."
Kim H., Feil I.K., Verlinde C.L.M.J., Petra P.H., Hol W.G.J.
Biochemistry 34:14975-14986(1995) [PubMed: 7578111] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD AND INORGANIC PHOSPHATE, SUBUNIT.
[3]"Crystal structure of Leishmania mexicana glycosomal glyceraldehyde-3-phosphate dehydrogenase in a new crystal form confirms the putative physiological active site structure."
Kim H., Hol W.G.J.
J. Mol. Biol. 278:5-11(1998) [PubMed: 9571030] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD AND INORGANIC PHOSPHATE, SUBUNIT.
[4]"Structure-based design of submicromolar, biologically active inhibitors of trypanosomatid glyceraldehyde-3-phosphate dehydrogenase."
Aronov A.M., Suresh S., Buckner F.S., van Voorhis W.C., Verlinde C.L., Opperdoes F.R., Hol W.G.J., Gelb M.H.
Proc. Natl. Acad. Sci. U.S.A. 96:4273-4278(1999) [PubMed: 10200252] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH ADENOSINE ANALOGS.
[5]"Conformational changes in Leishmania mexicana glyceraldehyde-3-phosphate dehydrogenase induced by designed inhibitors."
Suresh S., Bressi J.C., Kennedy K.J., Verlinde C.L.M.J., Gelb M.H., Hol W.G.J.
J. Mol. Biol. 309:423-435(2001) [PubMed: 11371162] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ADENOSINE ANALOGS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X65226 Genomic DNA. Translation: CAA46334.1.
X65226 Genomic DNA. Translation: CAA46333.1.
PIRA48445.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ27890.
SMRQ27890. Positions 2-359.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR020831. 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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR10836. GAP_DH. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3PG_LEIME
AccessionPrimary (citable) accession number: Q27890
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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