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UniProtKB/Swiss-Prot entry Q2NEN0

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

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Entry information
Entry name G3P_METST
Primary accession number Q2NEN0
Secondary accession numbers None
Integrated into Swiss-Prot on April 4, 2006
Sequence was last modified on February 7, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 25)
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: Msp_1346
From
Methanosphaera stadtmanae (strain DSM 3091) [TaxID: 339860] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanosphaera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.188.2.642-658.2006; PubMed=16385054 [NCBI, ExPASy, EBI, Israel, Japan]
Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R., Gottschalk G., Thauer R.K.;
"The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.";
J. Bacteriol. 188:642-658(2006).
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
CP000102; ABC57723.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_448366.1; -.
3D structure databases
ModBase Q2NEN0.
Enzyme and pathway databases
BioCyc MSTA339860:MSP_1346-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0043891; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity (inferred from electronic annotation from EC).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from HAMAP).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
Graphical view of domain structure.
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.
Genome annotation databases
GeneID 3855085; -.
GenomeReviews CP000102_GR; Msp_1346.
KEGG mst:Msp_1346; -.
NMPDR fig|339860.6.peg.1292; -.
Phylogenomic databases
HOGENOM Q2NEN0; -.
Genome annotation databases
CMR Q2NEN0; Msp_1346.
Other
ProtoNet Q2NEN0.
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   337  337     Glyceraldehyde-3-phosphate dehydrogenase. PRO_0000232392
NP_BIND   11    12  2     NAD (By similarity). 
REGION   140   142  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   194   195  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   141   141        Nucleophile (By similarity). 
BINDING   111   111        NAD; via amide nitrogen (By similarity). 
BINDING   169   169        NAD (By similarity). 
BINDING   301   301        NAD; via carbonyl oxygen (By similarity). 
Sequence information
Length: 337 AA [This is the length of the unprocessed precursor] Molecular weight: 36910 Da [This is the MW of the unprocessed precursor] CRC64: 71F5CD8AAECC35BF [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKSIGINGYG TIGKRVADAV SAQDDMKIVG VTKRTPDYEA KAAVEKGYDL YISVPERESQ 

        70         80         90        100        110        120 
FEEAGIEVAG TADELFEKLD LVVDCTPGGI GAQNKTDIYE KIGLKAIFEG GEDHDAIGSS 

       130        140        150        160        170        180 
FNAEANYADN IGEDYVRVVS CNTTGLCRTL KPIYDISGIK KVRAVMVRRG ADPSDVKKGP 

       190        200        210        220        230        240 
INSIVPTTEV PSHHGPDVQT IIDDINVMTM ALLVPTTLMH THNIMVELED KITTDDVLDA 

       250        260        270        280        290        300 
FENAHRVLPV QKSLKLGSTA EIMEYAKDLG RSRGDMYEIP VWKESVNIEN GELFYMQAVH 

       310        320        330 
QESDVVPENV DAIRAMLELE EDGEKSILKT NKAMGIL
Q2NEN0 in FASTA format

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