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 A3MTU1

[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 G3P_PYRCJ
Primary accession number A3MTU1
Secondary accession numbers None
Integrated into Swiss-Prot on September 11, 2007
Sequence was last modified on April 3, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 15)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase
Synonyms GAPDH
EC 1.2.1.59
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Gene name
Name: gap
OrderedLocusNames: Pcal_0632
From
Pyrobaculum calidifontis (strain JCM 11548 / VA1) [TaxID: 410359] [HAMAP proteome]
Taxonomy Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae; Pyrobaculum.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
"Complete sequence of Pyrobaculum calidifontis JCM 11548.";
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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
CP000561; ABO08058.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001055524.1; -.
3D structure databases
ModBase A3MTU1.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from HAMAP).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00559; -; 1.
PBIL [Tree]
InterPro IPR000173; GlycerAld_3-P_DHase.
IPR006436; Glyceraldehyde-3-P_DHase_2_arc.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000149; GAP_DH; 1.
ProDom PD007761; GAPDH_like; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01546; GAPDH-II_archae; 1.
PROSITE PS00071; GAPDH; 1.
BLOCKS A3MTU1.
Genome annotation databases
GeneID 4909422; -.
GenomeReviews CP000561_GR; Pcal_0632.
KEGG pcl:Pcal_0632; -.
CMR A3MTU1; Pcal_0632.
Other
ProtoNet A3MTU1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   344  344     Glyceraldehyde-3-phosphate dehydrogenase. PRO_0000300976
NP_BIND   11    12  2     NAD (By similarity). 
REGION   139   141  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   195   196  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   140   140        Nucleophile (By similarity). 
BINDING   110   110        NAD; via amide nitrogen (By similarity). 
BINDING   169   169        NAD (By similarity). 
BINDING   302   302        NAD; via carbonyl oxygen (By similarity). 
Sequence information
Length: 344 AA [This is the length of the unprocessed precursor] Molecular weight: 37895 Da [This is the MW of the unprocessed precursor] CRC64: B8F7652F67DF435A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIKVGVVGYG TIGKRIADAV ALQDDMRVVG VVKMTPDYEA KIAAARGFPV YTAADRVEKF 

        70         80         90        100        110        120 
KKAGIEVAGT VEDLVKASDV VVDASPEDVG RENKEKYYRQ LDKRYIFQGG EEADVAEVSF 

       130        140        150        160        170        180 
NALANYDEAR GKRYIRVVSC NTTGITRVLS ALLLNGIGIR KARIFIARRG ADPKEHKKGP 

       190        200        210        220        230        240 
INDVVPNPTA VPSHHGPDVQ TVLKDVDIVT MAVAVPVTIM HMHMAYIELD GPRSRDEVLE 

       250        260        270        280        290        300 
AFAKTPRIFL ADVGSGFQSL AQFIEYARDL GRPRGDFPEV AVFRDSVTVR GDELYLMYGV 

       310        320        330        340 
HQESIVVPEN VDAIRAALGV LPKWQSIEKT DKSLKLFTEG KRYA
A3MTU1 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 ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!