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Reviewed, UniProtKB/Swiss-Prot Q01558 (G3PC_LEIME)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

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

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Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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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.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 331330Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
PRO_0000145528

Regions

Nucleotide binding11 – 122NAD By similarity
Region148 – 1503Glyceraldehyde 3-phosphate binding By similarity
Region208 – 2092Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1491Nucleophile By similarity
Binding site331NAD By similarity
Binding site771NAD; via carbonyl oxygen By similarity
Binding site1791Glyceraldehyde 3-phosphate By similarity
Binding site2311Glyceraldehyde 3-phosphate By similarity
Binding site3131NAD By similarity
Site1761Activates thiol group during catalysis By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q01558-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DC2129BD57ABA5C7

FASTA33135,643
        10         20         30         40         50         60 
MVKVGINGFG RIGRVVFRAA QMRPDIEIVG INDLLDAEYM AYSLKYDSTH GRFDGTVEVI 

        70         80         90        100        110        120 
KGALVVNGKS IRVTSERDPA NLKWDEIGVE VVVESTGLFL TQETAHKHIE AGARRVVMTG 

       130        140        150        160        170        180 
PPKDDTPMFV MGVNHTTYKG QPIISNASCT TNCLAPLAKV VNEKYGIVEG LMTTVHATTA 

       190        200        210        220        230        240 
TQKTVDGPSL KDWRGGRGAS QNIIPSSTGA PKAVGKVYPA LDGKLTGMAF RVPTPNVSVV 

       250        260        270        280        290        300 
DLTVRLEKPA TYKDICAAIK AAAEGEMKGI LGYTDDEVVS SDFNGVALTS VFDVKAGISL 

       310        320        330 
NDHFVKLVSW YDNETGYSHK VLDLILHTSA R

« Hide

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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].

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Cross-references

Sequence databases

X65220 Genomic DNA. Translation: CAA46323.1.
PIRB48445.

3D structure databases

HSSPHSSP built from PDB template 1DC5 based on UniProtKB P06977.
SMRQ01558. Positions 2-329.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.12. 1480.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DH.
IPR006424. Glyceraldehyde-3-P_DH_1.
[Graphical view]
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.
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameG3PC_LEIME
AccessionPrimary (citable) accession number: Q01558
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 68 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents