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Reviewed, UniProtKB/Swiss-Prot P34923 (G3PC_PHYPA)

Last modified June 16, 2009. Version 57. 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
    EC=1.2.1.12
Gene names
Name: GAPC
OrganismPhyscomitrella patens (Moss)
Taxonomic identifier3218 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Bryophyta › Moss Superclass V › Bryopsida › Funariidae › Funariales › Funariaceae › Physcomitrella

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Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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

Chain1 – 342342Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
PRO_0000145613

Regions

Nucleotide binding16 – 172NAD By similarity
Region155 – 1573Glyceraldehyde 3-phosphate binding By similarity
Region215 – 2162Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1561Nucleophile By similarity
Binding site381NAD By similarity
Binding site851NAD; via carbonyl oxygen By similarity
Binding site1861Glyceraldehyde 3-phosphate By similarity
Binding site2381Glyceraldehyde 3-phosphate By similarity
Binding site3201NAD By similarity
Site1831Activates thiol group during catalysis By similarity

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Sequences

Sequence LengthMass (Da)Tools
P34923-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: F15CD336F1E4CFCA

FASTA34236,762
        10         20         30         40         50         60 
MVGSAKIKVG INGFGRIGRL VARVALERDD IELVAINDPF ITPEYMTYMF KYDSTHGQWK 

        70         80         90        100        110        120 
KTEVTLHSEG HLTFGGNPVA VYACRDPSEI PWGKHGADFV VESTGVFTDK DKAAAHLKGG 

       130        140        150        160        170        180 
AKKVVISAPS KDAPMFVMGV NENKYSDEDI VSNASCTTNC LAPLAKVIND KFGILEGLMT 

       190        200        210        220        230        240 
TVHATTATQK TVDGPSSKDW RGGRSAATNI IPSATGAAKA VGKVLPELNG KLTGMAFRVP 

       250        260        270        280        290        300 
TTDVSVVDLT VRLEKPASYD AIKTAIKEAS EGQMKGILGY TEDDVVSTDF ITDSRSSIFD 

       310        320        330        340 
AKAGIALSDT FVKLVAWYDN EWGYSNRVVD LIVHMAKQGT SQ

« Hide

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References

[1]"Molecular phylogenies in angiosperm evolution."
Martin W., Lydiate D., Brinkmann H., Forkmann G., Saedler H., Cerff R.
Mol. Biol. Evol. 10:140-162(1993) [PubMed: 8095691] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases

X72381 mRNA. Translation: CAA51071.1.

3D structure databases

HSSPHSSP built from PDB template 1DSS based on UniProtKB P56649.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.12. 3698.

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_PHYPA
AccessionPrimary (citable) accession number: P34923
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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