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UniProtKB/Swiss-Prot entry O34425


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

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Entry information
Entry name G3P2_BACSU
Primary accession number O34425
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 69)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase 2
Synonyms EC 1.2.1.59
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
GAPDH
Gene name
Name: gapB
OrderedLocusNames: BSU29020
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;
PubMed=9387221 [NCBI, ExPASy, EBI, Israel, Japan]
Lapidus A., Galleron N., Sorokin A., Ehrlich S.-D.;
"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region.";
Microbiology 143:3431-3441(1997).
[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]
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
AF008220; AAC00355.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99118; CAB14862.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G69628; G69628.
RefSeq NP_390780.1; -.
3D structure databases
HSSP P00362; 1NQO. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase O34425.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2898-MON; -.
Organism-specific databases
SubtiList BG12592; gapB. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0043891; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity (inferred from electronic annotation from EC).
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.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 2.
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 O34425.
ProtoNet O34425.
Genome annotation databases
GeneID 937393; -.
GenomeReviews AL009126_GR; BSU29020.
KEGG bsu:BSU29020; -.
NMPDR fig|224308.1.peg.2905; -.
Phylogenomic databases
HOGENOM O34425; -.
Genome annotation databases
CMR O34425; BSU29020.
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   340  340     Glyceraldehyde-3-phosphate dehydrogenase 2. PRO_0000145635
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   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: 340 AA [This is the length of the unprocessed precursor] Molecular weight: 37476 Da [This is the MW of the unprocessed precursor] CRC64: DD1DD4BC7D633EC6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKVKVAINGF GRIGRMVFRK AMLDDQIQVV AINASYSAET LAHLIKYDTI HGRYDKEVVA 

        70         80         90        100        110        120 
GEDSLIVNGK KVLLLNSRDP KQLPWREYDI DIVVEATGKF NAKDKAMGHI EAGAKKVILT 

       130        140        150        160        170        180 
APGKNEDVTI VMGVNEDQFD AERHVIISNA SCTTNCLAPV VKVLDEEFGI ESGLMTTVHA 

       190        200        210        220        230        240 
YTNDQKNIDN PHKDLRRARA CGESIIPTTT GAAKALSLVL PHLKGKLHGL ALRVPVPNVS 

       250        260        270        280        290        300 
LVDLVVDLKT DVTAEEVNEA FKRAAKTSMY GVLDYSDEPL VSTDYNTNPH SAVIDGLTTM 

       310        320        330        340 
VMEDRKVKVL AWYDNEWGYS CRVVDLIRHV AARMKHPSAV 

O34425 in FASTA format

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