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UniProtKB/Swiss-Prot entry P09124


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

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Entry information
Entry name G3P1_BACSU
Primary accession number P09124
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 82)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase 1
Synonyms EC 1.2.1.12
NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
GAPDH
Gene name
Name: gapA
Synonyms: gap
OrderedLocusNames: BSU33940
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / BD170;
DOI=10.1093/nar/17.3.1251; PubMed=2493629 [NCBI, ExPASy, EBI, Israel, Japan]
Viaene A., Dhaese P.;
"Sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from Bacillus subtilis.";
Nucleic Acids Res. 17:1251-1251(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
PROTEIN SEQUENCE OF 2-31.
STRAIN=168 / JH642;
PubMed=8755892 [NCBI, ExPASy, EBI, Israel, Japan]
Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
"Cold shock stress-induced proteins in Bacillus subtilis.";
J. Bacteriol. 178:4611-4619(1996).
[4]
CHARACTERIZATION.
DOI=10.1074/jbc.275.19.14031; PubMed=10799476 [NCBI, ExPASy, EBI, Israel, Japan]
Fillinger S., Boschi-Muller S., Azza S., Dervyn E., Branlant G., Aymerich S.;
"Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium.";
J. Biol. Chem. 275:14031-14037(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
X13011; CAA31434.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99121; CAB15399.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S02754; DEBSG.
RefSeq NP_391274.1; -.
3D structure databases
HSSP P00362; 1NQO. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
SMR P09124; 2-335.
ModBase P09124.
Enzyme and pathway databases
BioCyc BSUB224308:BSU3391-MON; -.
Organism-specific databases
SubtiList BG10827; gapA. [Micado]
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.
Genome annotation databases
GeneID 938627; -.
GenomeReviews AL009126_GR; BSU33940.
KEGG bsu:BSU33940; -.
NMPDR fig|224308.1.peg.3400; -.
Phylogenomic databases
HOGENOM P09124; -.
Genome annotation databases
CMR P09124; BSU33940.
Other
ProtoNet P09124.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
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   335  334     Glyceraldehyde-3-phosphate dehydrogenase 1. PRO_0000145634
NP_BIND   12    13  2     NAD (By similarity). 
REGION   151   153  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   210   211  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   152   152        Nucleophile (By similarity). 
BINDING   34    34        NAD (By similarity). 
BINDING   78    78        NAD; via carbonyl oxygen (By similarity). 
BINDING   182   182        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   197   197        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   233   233        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   315   315        NAD (By similarity). 
SITE   179   179  1     Activates thiol group during catalysis (By similarity). 
Sequence information
Length: 335 AA [This is the length of the unprocessed precursor] Molecular weight: 35833 Da [This is the MW of the unprocessed precursor] CRC64: B7A422A5CE3AD1DF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVKVGINGF GRIGRNVFRA ALNNPEVEVV AVNDLTDANM LAHLLQYDSV HGKLDAEVSV 

        70         80         90        100        110        120 
DGNNLVVNGK TIEVSAERDP AKLSWGKQGV EIVVESTGFF TKRADAAKHL EAGAKKVIIS 

       130        140        150        160        170        180 
APANEEDITI VMGVNEDKYD AANHDVISNA SCTTNCLAPF AKVLNDKFGI KRGMMTTVHS 

       190        200        210        220        230        240 
YTNDQQILDL PHKDYRRARA AAENIIPTST GAAKAVSLVL PELKGKLNGG AMRVPTPNVS 

       250        260        270        280        290        300 
LVDLVAELNQ EVTAEEVNAA LKEAAEGDLK GILGYSEEPL VSGDYNGNKN SSTIDALSTM 

       310        320        330 
VMEGSMVKVI SWYDNESGYS NRVVDLAAYI AKKGL 

P09124 in FASTA format

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