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Reviewed, UniProtKB/Swiss-Prot P34920 (G3PC_CHOCR)

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
OrganismChondrus crispus (Carragheen)
Taxonomic identifier2769 [NCBI]
Taxonomic lineageEukaryota › Rhodophyta › Florideophyceae › Gigartinales › Gigartinaceae › Chondrus

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Protein attributes

Sequence length335 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 – 335335Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
PRO_0000145597

Regions

Nucleotide binding13 – 142NAD By similarity
Region151 – 1533Glyceraldehyde 3-phosphate binding By similarity
Region211 – 2122Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1521Nucleophile By similarity
Binding site351NAD By similarity
Binding site801NAD; via carbonyl oxygen By similarity
Binding site1821Glyceraldehyde 3-phosphate By similarity
Binding site2341Glyceraldehyde 3-phosphate By similarity
Binding site3161NAD By similarity
Site1791Activates thiol group during catalysis By similarity

Experimental info

Sequence conflict2501A → T in CAA51517. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P34920-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: B09241EF399D397C

FASTA33536,054
        10         20         30         40         50         60 
MTAPKVGING FGRIGRLVLR AAIEKGTCQV VAINDPFIDL DYMAYMLKYD STHGRYAGDV 

        70         80         90        100        110        120 
SIKDGKLQVD GNSITVFAHR DPAEIPWATA AADYIVEATG VFTLKDKAAA HFKGGAKKVV 

       130        140        150        160        170        180 
ISAPSKDAPM FVCGVNEAKY TPDLDIISNA SCTTNCLAPL VKVIHEKYGI EEGLMTTVHA 

       190        200        210        220        230        240 
TTATQKTVDG PSNKDWRGGR GRGRNIIPSS TGAAKAVGKV MPELNGKLTG MAFRVPTPDV 

       250        260        270        280        290        300 
SVVDLTVRLA SETTYEDIKA TMKAAADDSM KGIMKYTEDA VVSTDFIHDD ASCIFDASAG 

       310        320        330 
IMLNSKFCKL VAWYDNEWGY SNRVVDLIAH ISKVQ

« Hide

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References

[1]"The evolutionary origin of red algae as deduced from the nuclear genes encoding cytosolic and chloroplast glyceraldehyde-3-phosphate dehydrogenases from Chondrus crispus."
Liaud M.-F., Valentin C., Martin W., Bouget F.Y., Kloareg B., Cerff R.
J. Mol. Evol. 38:319-327(1994) [PubMed: 8007000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: Stackhouse.

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Cross-references

Sequence databases

X73034 mRNA. Translation: CAA51515.1.
X73036 Genomic DNA. Translation: CAA51517.1.
PIRS43339.

3D structure databases

HSSPHSSP built from PDB template 1CRW based on UniProtKB P56649.
SMRP34920. Positions 5-334.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.12. 190989.

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_CHOCR
AccessionPrimary (citable) accession number: P34920
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)

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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