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 A5ULT9

[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_METS3
Primary accession number A5ULT9
Secondary accession numbers None
Integrated into Swiss-Prot on September 11, 2007
Sequence was last modified on July 10, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 14)
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: Msm_0962
From
Methanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861) [TaxID: 420247] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0704189104; PubMed=17563350 [NCBI, ExPASy, EBI, Israel, Japan]
Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
"Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut.";
Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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
CP000678; ABQ87167.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001273535.1; -.
3D structure databases
ModBase A5ULT9.
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.
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 A5ULT9.
ProtoNet A5ULT9.
Genome annotation databases
GeneID 5217242; -.
GenomeReviews CP000678_GR; Msm_0962.
KEGG msi:Msm_0962; -.
CMR A5ULT9; Msm_0962.
Other
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   338  338     Glyceraldehyde-3-phosphate dehydrogenase. PRO_0000300971
NP_BIND   11    12  2     NAD (By similarity). 
REGION   140   142  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   195   196  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   302   302        NAD; via carbonyl oxygen (By similarity). 
Sequence information
Length: 338 AA [This is the length of the unprocessed precursor] Molecular weight: 37130 Da [This is the MW of the unprocessed precursor] CRC64: C534794D04B1BA6E [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKSVAINGYG TIGKRVADAV AAQDDMKVIG VSKTRPNYES RTAVEEKGYD LYIGIPERAD 

        70         80         90        100        110        120 
QFKEAGIEIA GTVEDMIQEA DVVVDCTPGT IGPQNLEMYK KAGVKAIYQG GEDHELTGLS 

       130        140        150        160        170        180 
FNAISNYDDS YGKDYTRVVS CNTTGLTRTL STIDPIADIK KVRAVMVRRG SDPSEVKKGP 

       190        200        210        220        230        240 
INSIVPNPPK VPSHHGPDVK TVMEGIDVTT MALLVPTTLM HQHNIMVEIN NEVETQEIID 

       250        260        270        280        290        300 
ALEKRSRVLV VDASEGLGST AELMEYAKEL GRNRNDLYEI PVWRESINVV GNELYYMQAV 

       310        320        330 
HQESDVVPEN IDAIRALLEM ESDNEKSIAK TNKAMGIL
A5ULT9 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!