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UniProtKB/Swiss-Prot entry P00362

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

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Entry information
Entry name G3P_BACST
Primary accession number P00362
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 5)
Annotations were last modified on    November 25, 2008 (Entry version 89)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase
Synonyms GAPDH
EC 1.2.1.12
Gene name
Name: gap
From
Bacillus stearothermophilus (Geobacillus stearothermophilus) [TaxID: 1422] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(89)90049-8; PubMed=2684782 [NCBI, ExPASy, EBI, Israel, Japan]
Tesfay H.S., Amelunxen R.E., Goldberg I.D.;
"Nucleotide sequences of genes encoding heat-stable and heat-labile glyceraldehyde-3-phosphate dehydrogenases; amino acid sequence and protein thermostability.";
Gene 82:237-248(1989).
[2]
 ERRATUM, AND RETRACTION.
DOI=10.1016/0378-1119(90)90484-9; PubMed=2227448 [NCBI, ExPASy, EBI, Israel, Japan]
Tesfay H.S., Amelunxen R.E., Goldberg I.D.;
Gene 94:144-144(1990).
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(89)90391-0; PubMed=2656407 [NCBI, ExPASy, EBI, Israel, Japan]
Branlant C., Oster T., Branlant G.;
"Nucleotide sequence determination of the DNA region coding for Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase and of the flanking DNA regions required for its expression in Escherichia coli.";
Gene 75:145-155(1989).
[4]
 PROTEIN SEQUENCE OF 2-335.
PubMed=7408868 [NCBI, ExPASy, EBI, Israel, Japan]
Walker J.E., Carne A.F., Runswick M.J., Bridgen J., Harris J.I.;
"D-glyceraldehyde-3-phosphate dehydrogenase. Complete amino-acid sequence of the enzyme from Bacillus stearothermophilus.";
Eur. J. Biochem. 108:549-565(1980).
[5]
 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
DOI=10.1038/266328a0; PubMed=193030 [NCBI, ExPASy, EBI, Israel, Japan]
Biesecker G., Harris J.I., Thierry J.-C., Walker J.E., Wonacott A.J.;
"Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus.";
Nature 266:328-333(1977).
[6]
 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
DOI=10.1016/0022-2836(87)90635-8; PubMed=3586018 [NCBI, ExPASy, EBI, Israel, Japan]
Skarzynski T., Moody P.C.E., Wonacott A.J.;
"Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8-A resolution.";
J. Mol. Biol. 193:171-187(1987).
[7]
 X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH NAD, MUTAGENESIS OF CYS-152, AND SUBUNIT.
DOI=10.1006/jmbi.1997.0998; PubMed=9175858 [NCBI, ExPASy, EBI, Israel, Japan]
Didierjean C., Rahuel-Clermont S., Vitoux B., Dideberg O., Branlant G., Aubry A.;
"A crystallographic comparison between mutated glyceraldehyde-3-phosphate dehydrogenases from Bacillus stearothermophilus complexed with either NAD+ or NADP+.";
J. Mol. Biol. 268:739-759(1997).
[8]
 X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NAD AND GLYCERALDEHYDE 3-PHOSPHATE.
DOI=10.1074/jbc.M211040200; PubMed=12569100 [NCBI, ExPASy, EBI, Israel, Japan]
Didierjean C., Corbier C., Fatih M., Favier F., Boschi-Muller S., Branlant G., Aubry A.;
"Crystal structure of two ternary complexes of phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus with NAD and D-glyceraldehyde 3-phosphate.";
J. Biol. Chem. 278:12968-12976(2003).
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
M24493; AAA22461.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JS0164; DEBSGF.
3D structure databases
PDB
1DBV; X-ray; 2.50 A; O/P/Q/R=1-335.[ExPASy / RCSB / EBI]
1GD1; X-ray; 1.80 A; O/P/Q/R=1-335.[ExPASy / RCSB / EBI]
1NPT; X-ray; 2.18 A; O/P/Q/R=1-335.[ExPASy / RCSB / EBI]
1NQ5; X-ray; 2.11 A; A/C/O/Q=1-335.[ExPASy / RCSB / EBI]
1NQA; X-ray; 2.20 A; O/P/Q/R=1-335.[ExPASy / RCSB / EBI]
1NQO; X-ray; 2.01 A; A/C/O/Q=1-335.[ExPASy / RCSB / EBI]
2DBV; X-ray; 2.20 A; O/P/Q/R=1-335.[ExPASy / RCSB / EBI]
2GD1; X-ray; 2.50 A; O/P/Q/R=1-335.[ExPASy / RCSB / EBI]
3CMC; X-ray; 1.77 A; O/P/Q/R=2-335.[ExPASy / RCSB / EBI]
3DBV; X-ray; 2.45 A; O/P/Q/R=1-335.[ExPASy / RCSB / EBI]
4DBV; X-ray; 2.50 A; O/P/Q/R=1-335.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DBV; -.
1GD1; -.
1NPT; -.
1NQ5; -.
1NQA; -.
1NQO; -.
2DBV; -.
2GD1; -.
3CMC; -.
3DBV; -.
4DBV; -.
ModBase P00362.
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.
ProtoNet P00362.
Other
SWISS-3DIMAGE P00362.
LinkHub P00362; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   335  334     Glyceraldehyde-3-phosphate dehydrogenase. PRO_0000145633
NP_BIND   12    13  2     NAD. 
REGION   151   153  3     Glyceraldehyde 3-phosphate binding. 
ACT_SITE   152   152        Nucleophile. 
BINDING   34    34        NAD. 
BINDING   78    78        NAD; via carbonyl oxygen. 
BINDING   120   120        NAD. 
BINDING   182   182        Glyceraldehyde 3-phosphate. 
BINDING   197   197        Glyceraldehyde 3-phosphate. 
BINDING   233   233        Glyceraldehyde 3-phosphate. 
BINDING   315   315        NAD. 
SITE   179   179  1     Activates thiol group during catalysis. 
MUTAGEN   152   152        C->A: Loss of activity. 
STRAND   3     8  6      
HELIX   12    21  10      
STRAND   25    33  9      
HELIX   38    46  9      
TURN   49    51  3      
STRAND   58    61  4      
STRAND   64    67  4      
STRAND   70    75  6      
HELIX   80    82  3      
HELIX   85    88  4      
STRAND   92    95  4      
STRAND   97    99  3      
HELIX   103   106  4      
HELIX   108   111  4      
STRAND   115   121  7      
STRAND   127   129  3      
TURN   132   134  3      
HELIX   136   138  3      
TURN   141   143  3      
STRAND   146   148  3      
HELIX   152   168  17      
STRAND   170   180  11      
STRAND   185   189  5      
TURN   195   198  4      
TURN   201   203  3      
STRAND   206   209  4      
HELIX   214   218  5      
HELIX   221   223  3      
TURN   224   226  3      
STRAND   227   235  9      
STRAND   240   250  11      
HELIX   254   266  13      
TURN   267   269  3      
STRAND   273   276  4      
HELIX   282   285  4      
STRAND   290   295  6      
HELIX   296   298  3      
STRAND   300   302  3      
TURN   303   305  3      
STRAND   306   313  8      
HELIX   317   332  16      
Sequence information
Length: 335 AA [This is the length of the unprocessed precursor] Molecular weight: 36075 Da [This is the MW of the unprocessed precursor] CRC64: DBAAA2DD24497E18 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAVKVGINGF GRIGRNVFRA ALKNPDIEVV AVNDLTDANT LAHLLKYDSV HGRLDAEVSV 

        70         80         90        100        110        120 
NGNNLVVNGK EIIVKAERDP ENLAWGEIGV DIVVESTGRF TKREDAAKHL EAGAKKVIIS 

       130        140        150        160        170        180 
APAKNEDITI VMGVNQDKYD PKAHHVISNA SCTTNCLAPF AKVLHEQFGI VRGMMTTVHS 

       190        200        210        220        230        240 
YTNDQRILDL PHKDLRRARA AAESIIPTTT GAAKAVALVL PELKGKLNGM AMRVPTPNVS 

       250        260        270        280        290        300 
VVDLVAELEK EVTVEEVNAA LKAAAEGELK GILAYSEEPL VSRDYNGSTV SSTIDALSTM 

       310        320        330 
VIDGKMVKVV SWYDNETGYS HRVVDLAAYI ASKGL
P00362 in FASTA format

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