ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P25861

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name G3PC_ANTMA
Primary accession number P25861
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on May 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 57)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase, cytosolic
Synonym EC 1.2.1.12
Gene name
Name: GAPC
Synonyms: GAPDH
From
Antirrhinum majus (Garden snapdragon) [TaxID: 4151] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
Martin W., Gierl A., Seadler H.;
"Molecular evidence for pre-Cretaceous angiosperm origins.";
Nature 339:46-48(1989).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X59517; CAA42103.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S17991; DESKG.
3D structure databases
HSSP P56649; 1IHX. [HSSP ENTRY / PDB]
ModBase P25861.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
Graphical view of domain structure.
PANTHER PTHR10836; GAP_DH; 1.
Pfam PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000149; GAP_DH; 1.
PRINTS PR00078; G3PDHDRGNASE.
TIGRFAMs TIGR01534; GAPDH-I; 1.
PROSITE PS00071; GAPDH; 1.
BLOCKS P25861.
ProtoNet P25861.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Glycolysis; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   337  337     Glyceraldehyde-3-phosphate dehydrogenase, cytosolic. PRO_0000145593
NP_BIND   13    14  2     NAD (By similarity). 
REGION   153   155  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   213   214  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   154   154        Nucleophile (By similarity). 
BINDING   35    35        NAD (By similarity). 
BINDING   82    82        NAD; via carbonyl oxygen (By similarity). 
BINDING   184   184        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   236   236        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   318   318        NAD (By similarity). 
SITE   181   181  1     Activates thiol group during catalysis (By similarity). 
Sequence information
Length: 337 AA [This is the length of the unprocessed precursor] Molecular weight: 36685 Da [This is the MW of the unprocessed precursor] CRC64: 0E0E69F1F474F0D7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAPIKIGING FGRIGRLVAR VALQRDDVEL VAVNDPFIST DYMTYMFKYD SVHGAWKHHE 

        70         80         90        100        110        120 
LKVKDEKTLL FGEKPVVVFG RRNPEEIPRA STGAEYIVES TGVFTDKDKA AAHLKGGAKK 

       130        140        150        160        170        180 
VIISAPSKDA PMFVVGVNEK EYKSDLHIVS NASCTTNCLA PLAKVINDRF GIVEGLMTTV 

       190        200        210        220        230        240 
HSITATQKTV DGPSAKDWRG GRAASFNIIP SSTGAAKAVG KVLPQLNGKL TGMSFRVPTV 

       250        260        270        280        290        300 
DVSVVDLTVR LEKKATYEQI KAAIKEESEG KLKGILGYTE DDVVSTDFVG DSRSSIFDAK 

       310        320        330 
AGIALNDNFV KLVSWYDNEW GYSTRVVDLI VHMASVQ
P25861 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by au flag APAF Australia Mirror sites: Brazil Canada China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!