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Reviewed, UniProtKB/Swiss-Prot P08735 (G3PC_MAIZE)

Last modified November 25, 2008. Version 71. 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 1
    EC=1.2.1.12
Gene names
Name: GAPC1
Synonyms: GAPC, GPC1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACCAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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

Plants contain three forms of GAPDH: a cytosolic form which participates in glycolysis and two chloroplast forms 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-KW

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Glyceraldehyde-3-phosphate dehydrogenase, cytosolic 1
PRO_0000145605

Regions

Nucleotide binding13 – 142NAD By similarity
Region1 – 151151Binding to NAD
Region152 – 337186Catalytic
Region153 – 1553Glyceraldehyde 3-phosphate binding By similarity
Region213 – 2142Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1541Nucleophile By similarity
Binding site351NAD By similarity
Binding site821NAD; via carbonyl oxygen 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

Experimental info

Sequence conflict3361T → S in CAA30151. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P08735-1 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: E18F580F09FDC07B

FASTA33736,523
        10         20         30         40         50         60 
MGKIKIGING FGRIGRLVAR VALQSEDVEL VAVNDPFITT DYMTYMFKYD TVHGHWKHSD 

        70         80         90        100        110        120 
ITLKDSKTLL FGDKPVTVFG IRNPEEIPWG EAGAEYVVES TGVFTDKDKA AAHLKGGAKK 

       130        140        150        160        170        180 
VVISAPSKDA PMFVVGVNED KYTSDVNIVS NASCTTNCLA PLAKVIHDNF GIVEGLMTTV 

       190        200        210        220        230        240 
HAITATQKTV DGPSAKDWRG GRAASFNIIP SSTGAAKAVG KVLPDLNGKL TGMSFRVPTV 

       250        260        270        280        290        300 
DVSVVDLTVR IEKGASYEDI KKAIKAASEG PLKGIMGYVE EDLVSTDFLG DSRSSIFDAK 

       310        320        330 
AGIALNDHFV KLVSWYDNEW GYSNRVVDLI RHMFKTQ 

« Hide

References

[1]"Structure, evolution and anaerobic regulation of a nuclear gene encoding cytosolic glyceraldehyde-3-phosphate dehydrogenase from maize."
Martinez P., Martin W.F., Cerff R.
J. Mol. Biol. 208:551-565(1989) [PubMed: 2810356] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Wisconsin 22.
[2]"Endosymbiotic origin and codon bias of the nuclear gene for chloroplast glyceraldehyde-3-phosphate dehydrogenase from maize."
Brinkmann H., Martinez P., Quigley F., Martin W.F., Cerff R.
J. Mol. Evol. 26:320-328(1987) [PubMed: 3131533] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

X07156 mRNA. Translation: CAA30151.1.
X15596 Genomic DNA. Translation: CAA33620.1.
PIRDEZMGC. S00354.
RefSeqNP_001105413.1.
UniGeneZm.3765

3D structure databases

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

Genome annotation databases

GeneID542367.

Organism-specific databases

GrameneP08735.
MaizeGDB13873.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DHase.
IPR006424. Glyceraldehyde-3-P_DHase_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_MAIZE
AccessionPrimary (citable) accession number: P08735
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 1, 1990
Last modified: November 25, 2008
This is version 71 of the entry and version 2 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