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UniProtKB/Swiss-Prot entry P0A9B2


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

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Entry information
Entry name G3P1_ECOLI
Primary accession number P0A9B2
Secondary accession number P06977
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 41)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase A
Synonyms GAPDH-A
EC 1.2.1.12
Gene name
Name: gapA
OrderedLocusNames: b1779, JW1768
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2990926 [NCBI, ExPASy, EBI, Israel, Japan]
Branlant G., Branlant C.;
"Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase.";
Eur. J. Biochem. 150:61-66(1985).
[2]
SEQUENCE REVISION TO 295-300.
Nelson K.;
Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan]
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
Submitted (SEP-1994) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-314.
STRAIN=A8190, E2666-74, E3406, E830587, E851819, ECOR 14, ECOR 32, ECOR 40, ECOR 52, ECOR 58, ECOR 64, and ECOR 70;
PubMed=1862091 [NCBI, ExPASy, EBI, Israel, Japan]
Nelson K., Whittam T.S., Selander R.K.;
"Nucleotide polymorphism and evolution in the glyceraldehyde-3-phosphate dehydrogenase gene (gapA) in natural populations of Salmonella and Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 88:6667-6671(1991).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-321.
STRAIN=ECOR 10, ECOR 16, ECOR 38, ECOR 39, ECOR 4, ECOR 40, ECOR 49, ECOR 65, ECOR 68, ECOR 8, and O2:HN / ECOR 50 / P97 / UPEC;
PubMed=7896119 [NCBI, ExPASy, EBI, Israel, Japan]
Guttman D.S., Dykhuizen D.E.;
"Detecting selective sweeps in naturally occurring Escherichia coli.";
Genetics 138:993-1003(1994).
[10]
GENE TRANSFER DISCUSSION.
DOI=10.1007/BF02106053; PubMed=2124629 [NCBI, ExPASy, EBI, Israel, Japan]
Doolittle R.F., Feng D.F., Anderson K.L., Alberro M.R.;
"A naturally occurring horizontal gene transfer from a eukaryote to a prokaryote.";
J. Mol. Evol. 31:383-388(1990).
[11]
MUTAGENESIS OF HIS-177.
DOI=10.1021/bi00432a036; PubMed=2659073 [NCBI, ExPASy, EBI, Israel, Japan]
Soukri A., Mougin A., Corbier C., Wonacott A., Branlant C., Branlant G.;
"Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis.";
Biochemistry 28:2586-2592(1989).
[12]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1006/jmbi.1996.0204; PubMed=8636984 [NCBI, ExPASy, EBI, Israel, Japan]
Duee E., Olivier-Deyris L., Fanchon E., Corbier C., Branlant G., Dideberg O.;
"Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity.";
J. Mol. Biol. 257:814-838(1996).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND GLYCERALDEHYDE 3-PHOSPHATE, AND SUBUNIT.
DOI=10.1021/bi9927080; PubMed=10978154 [NCBI, ExPASy, EBI, Israel, Japan]
Yun M., Park C.-G., Kim J.-Y., Park H.-W.;
"Structural analysis of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli: direct evidence of substrate binding and cofactor-induced conformational changes.";
Biochemistry 39:10702-10710(2000).
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
X02662; CAA26498.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74849.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15576.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66870; AAA23838.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66871; AAA23839.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66872; AAA02930.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66873; AAA23840.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66874; AAA23841.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66875; AAA23842.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66876; AAA23843.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66877; AAA23844.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66878; AAA23845.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66879; AAA23846.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66880; AAA23847.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66881; AAA23848.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M66882; AAA23849.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07750; AAC43271.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07751; AAC43272.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07752; AAC43273.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07754; AAC43274.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07765; AAC43284.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07768; AAC43285.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07769; AAC43286.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07770; AAC43287.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07771; AAC43288.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07772; AAC43289.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U07773; AAC43290.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A25209; DEECG3.
RefSeq AP_002398.1; -.
NP_416293.1; -.
3D structure databases
PDB
1DC3; X-ray; 2.50 A; A/B=1-331.[ExPASy / RCSB / EBI]
1DC4; X-ray; 2.50 A; A/B=1-331.[ExPASy / RCSB / EBI]
1DC5; X-ray; 2.00 A; A/B=1-331.[ExPASy / RCSB / EBI]
1DC6; X-ray; 2.00 A; A/B=1-331.[ExPASy / RCSB / EBI]
1GAD; X-ray; 1.80 A; O/P=1-331.[ExPASy / RCSB / EBI]
1GAE; X-ray; 2.17 A; O/P=1-331.[ExPASy / RCSB / EBI]
1S7C; X-ray; 2.04 A; A=1-331.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DC3; -.
1DC4; -.
1DC5; -.
1DC6; -.
1GAD; -.
1GAE; -.
1S7C; -.
ModBase P0A9B2.
Protein-protein interaction databases
IntAct P0A9B2; -.
Enzyme and pathway databases
BioCyc EcoCyc:GAPDH-A-MON; -.
MetaCyc:GAPDH-A-MON; -.
2D gel databases
SWISS-2DPAGE P0A9B2; -.
2DBase-Ecoli P0A9B2; -.
ECO2DBASE H034.3; 6TH EDITION.
I033.5; 6TH EDITION.
Organism-specific databases
EchoBASE EB0362; -.
EcoGene EG10367; gapA.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
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.
BLOCKS P0A9B2.
Genome annotation databases
GeneID 947679; -.
GenomeReviews U00096_GR; b1779.
AP009048_GR; JW1768.
KEGG ecj:JW1768; -.
eco:b1779; -.
Phylogenomic databases
HOGENOM P0A9B2; -.
Other
LinkHub P0A9B2; -.
Genome annotation databases
CMR P0A9B2; b1779.
Other
ProtoNet P0A9B2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; 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   331  330     Glyceraldehyde-3-phosphate dehydrogenase A. PRO_0000145648
NP_BIND   12    13  2     NAD (By similarity). 
REGION   149   151  3     Glyceraldehyde 3-phosphate binding. 
REGION   209   210  2     Glyceraldehyde 3-phosphate binding. 
ACT_SITE   150   150        Nucleophile. 
BINDING   34    34        NAD. 
BINDING   78    78        NAD; via carbonyl oxygen. 
BINDING   180   180        Glyceraldehyde 3-phosphate. 
BINDING   232   232        Glyceraldehyde 3-phosphate. 
BINDING   314   314        NAD. 
SITE   177   177  1     Activates thiol group during catalysis. 
VARIANT   43    43  1     Y -> I (in strain: ECOR 70). 
VARIANT   266   266  1     G -> D (in strain: E830587). 
VARIANT   267   267  1     E -> A (in strain: E2666-74). 
MUTAGEN   177   177        H->N: Reduces activity about 50-fold. 
STRAND   3     8  6      
HELIX   12    22  11      
STRAND   25    36  12      
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   111  9      
STRAND   115   121  7      
STRAND   124   126  3      
TURN   132   134  3      
STRAND   143   146  4      
HELIX   150   166  17      
STRAND   168   178  11      
STRAND   183   187  5      
HELIX   195   197  3      
TURN   200   202  3      
STRAND   205   208  4      
HELIX   211   218  8      
HELIX   220   222  3      
TURN   223   225  3      
STRAND   226   234  9      
STRAND   239   249  11      
HELIX   253   265  13      
TURN   266   271  6      
STRAND   272   275  4      
HELIX   281   284  4      
STRAND   289   294  6      
TURN   295   297  3      
STRAND   299   302  4      
STRAND   305   312  8      
HELIX   316   328  13      
Sequence information
Length: 331 AA [This is the length of the unprocessed precursor] Molecular weight: 35532 Da [This is the MW of the unprocessed precursor] CRC64: B3A460AA6D59E46D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTIKVGINGF GRIGRIVFRA AQKRSDIEIV AINDLLDADY MAYMLKYDST HGRFDGTVEV 

        70         80         90        100        110        120 
KDGHLIVNGK KIRVTAERDP ANLKWDEVGV DVVAEATGLF LTDETARKHI TAGAKKVVMT 

       130        140        150        160        170        180 
GPSKDNTPMF VKGANFDKYA GQDIVSNASC TTNCLAPLAK VINDNFGIIE GLMTTVHATT 

       190        200        210        220        230        240 
ATQKTVDGPS HKDWRGGRGA SQNIIPSSTG AAKAVGKVLP ELNGKLTGMA FRVPTPNVSV 

       250        260        270        280        290        300 
VDLTVRLEKA ATYEQIKAAV KAAAEGEMKG VLGYTEDDVV STDFNGEVCT SVFDAKAGIA 

       310        320        330 
LNDNFVKLVS WYDNETGYSN KVLDLIAHIS K 

P0A9B2 in FASTA format

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View entry in raw text format (no links)
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