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Reviewed, UniProtKB/Swiss-Prot P49644 (G3PC_CHLRE)

Last modified June 16, 2009. Version 62. 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

Names and origin

Protein namesRecommended name:
    Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
    EC=1.2.1.12
Gene names
Name: GAPC
OrganismChlamydomonas reinhardtii
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

Miscellaneous

Algae contain three forms of GAPDH: two cytosolic forms which participate in glycolysis and one chloroplastic form which participates in photosynthesis. These three forms are encoded by distinct genes.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
PRO_0000145596

Regions

Nucleotide binding14 – 152NAD By similarity
Region153 – 1553Glyceraldehyde 3-phosphate binding By similarity
Region213 – 2142Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1541Nucleophile By similarity
Binding site361NAD By similarity
Binding site1841Glyceraldehyde 3-phosphate By similarity
Binding site2361Glyceraldehyde 3-phosphate By similarity
Binding site3181NAD By similarity
Site1811Activates thiol group during catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P49644-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: A081514C3B13E2F7

FASTA34136,559
        10         20         30         40         50         60 
MSGKIKIGIN GFGRIGRLVM RATMLRPDIE VVAINDPFID AEYMAYMFKY DSVHKTWPGH 

        70         80         90        100        110        120 
VNGSKDGFLV EGRKIHTFTE SDPSKINWGA AGADIVIEST GVFTDIAKAT AHLTGGAKKV 

       130        140        150        160        170        180 
IITAPSNDAP MYVMGVNHEK YNPATDHIIS NASCTTNCLA PLAKVVNSKF GIKEGLMTTV 

       190        200        210        220        230        240 
HATTATQKTV DGPSKKDWRG GRAVNGNIIP SSTGAAKAVG KVLPELKGKL TGMAFRVPTN 

       250        260        270        280        290        300 
DVSVVDLTVT LEKATTYEDI MKALKEASEG EMKGVLAYTD EDVVSSDFVT DPASCTVDAK 

       310        320        330        340 
AGIMLSPTFV KLVAWYDNEW GYSNRVVDLA LHVAKKAAVK V 

« Hide

References

[1]"Five identical intron positions in ancient duplicated genes of eubacterial origin."
Kersanach R., Brinkmann H., Liaud M.-F., Zhang D.-X., Martin W., Cerff R.
Nature 367:387-389(1994) [PubMed: 8114942] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 1132.

Cross-references

Sequence databases

L27669 Genomic DNA. Translation: AAA86856.1.
PIRT08147.

3D structure databases

HSSPHSSP built from PDB template 1DC5 based on UniProtKB P06977.
ModBaseSearch...

Proteomic databases

PRIDEP49644.

Enzyme and pathway databases

BRENDA1.2.1.12. 144.

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...

Entry information

Entry nameG3PC_CHLRE
AccessionPrimary (citable) accession number: P49644
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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