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Reviewed, UniProtKB/Swiss-Prot P24751 (G3P1_ESCVU)

Last modified June 16, 2009. Version 60. 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
      Short name=GAPDH
    EC=1.2.1.12
Gene names
Name: gap
OrganismEscherichia vulneris
Taxonomic identifier566 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length294 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
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
   PTMAcetylation
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

Chain‹1 – ›294›294Glyceraldehyde-3-phosphate dehydrogenase
PRO_0000145659

Regions

Region134 – 1363Glyceraldehyde 3-phosphate binding By similarity
Region194 – 1952Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1351Nucleophile By similarity
Binding site191NAD By similarity
Binding site631NAD; via carbonyl oxygen By similarity
Binding site1651Glyceraldehyde 3-phosphate By similarity
Binding site2171Glyceraldehyde 3-phosphate By similarity
Site1621Activates thiol group during catalysis By similarity

Amino acid modifications

Modified residue1771N6-acetyllysine By similarity
Modified residue2341N6-acetyllysine By similarity

Experimental info

Non-terminal residue11
Non-terminal residue2941

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Sequences

Sequence LengthMass (Da)Tools
P24751-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 270A233457394730

FASTA29431,365
        10         20         30         40         50         60 
IVFRAAQKRS DIEIVAINDL LDAEYMAYML KYDSTHGRFD GTVEVKDGHL VVNGKKIRVT 

        70         80         90        100        110        120 
AERDPANLKW DEVGVDVVAE ATGIFLTDET ARKHITAGAK KVVLTGPSKD NTPMFVRGAN 

       130        140        150        160        170        180 
FDTYAGQDIV SNASCTTNCL APLAKVINDN FGIVEGLMTT VHATTATQKT VDGPSHKDWR 

       190        200        210        220        230        240 
GGRGAAQNII PSSTGAAKAV GKVLPELNGK LTGMAFRVPT PNVSVVDLTV RLEKAASYEE 

       250        260        270        280        290 
IKKAIKAASE GAMKGVLGYT EDDVVSTDFN GEVCTSVFDA KAGIALNDNF VKLV

« Hide

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References

[1]"Molecular and evolutionary relationships among enteric bacteria."
Lawrence J.G., Ochman H., Hartl D.L.
J. Gen. Microbiol. 137:1911-1921(1991) [PubMed: 1955870] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29943 / CDC 2898-73.

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Cross-references

Sequence databases

M63363 Genomic DNA. Translation: AAA23850.1.
PIRI41221.

3D structure databases

HSSPHSSP built from PDB template 1DC5 based on UniProtKB P06977.
SMRP24751. Positions 1-294.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.12. 297355.

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 nameG3P1_ESCVU
AccessionPrimary (citable) accession number: P24751
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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