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 P34919

[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 G3PA_CHOCR
Primary accession number P34919
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 58)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase, chloroplastic [Precursor]
Synonyms EC 1.2.1.13
NADP-dependent glyceraldehydephosphate dehydrogenase
Gene name
Name: GAPA
From
Chondrus crispus (Carragheen) [TaxID: 2769] 
Taxonomy Eukaryota; Rhodophyta; Florideophyceae; Gigartinales; Gigartinaceae; Chondrus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Stackhouse;
DOI=10.1007/BF00163149; PubMed=8007000 [NCBI, ExPASy, EBI, Israel, Japan]
Liaud M.-F., Valentin C., Martin W., Bouget F.Y., Kloareg B., Cerff R.;
"The evolutionary origin of red algae as deduced from the nuclear genes encoding cytosolic and chloroplast glyceraldehyde-3-phosphate dehydrogenases from Chondrus crispus.";
J. Mol. Evol. 38:319-327(1994).
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
X73035; CAA51516.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P19866; 1NBO. [HSSP ENTRY / PDB]
SMR P34919; 78-414.
ModBase P34919.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0047100; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity (inferred from electronic annotation from EC).
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:0006006; Biological process: glucose metabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019253; Biological process: reductive pentose-phosphate cycle (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.
PRINTS PR00078; G3PDHDRGNASE.
TIGRFAMs TIGR01534; GAPDH-I; 1.
PROSITE PS00071; GAPDH; 1.
ProtoNet P34919.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calvin cycle; Chloroplast; NADP; Oxidoreductase; Plastid; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    76  76     Chloroplast (Potential). 
CHAIN   77   414  338     Glyceraldehyde-3-phosphate dehydrogenase, chloroplastic. PRO_0000010419
NP_BIND   88    89  2     NADP (By similarity). 
REGION   230   232  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   289   290  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   231   231        Nucleophile (By similarity). 
BINDING   112   112        NADP (By similarity). 
BINDING   156   156        NADP; via carbonyl oxygen (By similarity). 
BINDING   261   261        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   276   276        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   312   312        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   394   394        NADP (By similarity). 
SITE   258   258  1     Activates thiol group during catalysis (By similarity). 
Sequence information
Length: 414 AA [This is the length of the unprocessed precursor] Molecular weight: 44459 Da [This is the MW of the unprocessed precursor] CRC64: 065DE62CE1064111 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAFVAPVATV RATTKSSVCQ VQGRSTFAQF SGMKKVNQSS RLQPAQSGSA FGGYSDANDA 

        70         80         90        100        110        120 
FYTRVSGIVA ATFGPTMKVR VAINGFGRIG RNFIRCWAGR SDSNMEVVCI NDTSGVKTAS 

       130        140        150        160        170        180 
HLLKYDSILG TFDADVSAGE DTISVNGKTI KIVSNRNPLQ LPWKEMNIDI VVEATGVFVD 

       190        200        210        220        230        240 
APGAGKHIEA GAKKVLITAP GKGDGIGTFV VGVNEKDYSH DKYDIVSNAS CTTNCMAPFM 

       250        260        270        280        290        300 
KVLDDEFGVV RGMMTTTHSY TGDQRLLDAG HRDLRRARSA ALNIVPTTTG AAKAVALVVP 

       310        320        330        340        350        360 
SLKGKLNGIA LRVPTPNVSV CDVVMQVNKK TFKEEVNGAL LKASEGAMKG IIKYSDEPLV 

       370        380        390        400        410 
SCDHRGTDES TIIDSSLTMV MGDDMIKVVA WYDNEWGYSQ RVVDLGEVMA RQWK
P34919 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 ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!