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 P08164


[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 NADE_BACSU
Primary accession number P08164
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 5)
Annotations were last modified on    November 4, 2008 (Entry version 82)
Name and origin of the protein
Protein name NH(3)-dependent NAD(+) synthetase
Synonyms EC 6.3.1.5
Spore outgrowth factor B
Sporulation protein outB
General stress protein 38
GSP38
Gene name
Name: nadE
Synonyms: outB
OrderedLocusNames: BSU03130
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].
PubMed=2435704 [NCBI, ExPASy, EBI, Israel, Japan]
Albertini A.M., Caramori T., Henner D.J., Ferrari E., Galizzi A.;
"Nucleotide sequence of the outB locus of Bacillus subtilis and regulation of its expression.";
J. Bacteriol. 169:1480-1484(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8969502 [NCBI, ExPASy, EBI, Israel, Japan]
Yamane K., Kumano M., Kurita K.;
"The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes.";
Microbiology 142:3047-3056(1996).
[3]
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).
[4]
PROTEIN SEQUENCE OF 2-19.
STRAIN=168 / IS58;
DOI=10.1002/elps.1150180820; PubMed=9298659 [NCBI, ExPASy, EBI, Israel, Japan]
Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis.";
Electrophoresis 18:1451-1463(1997).
[5]
PROTEIN SEQUENCE OF 2-11, AND PHOSPHORYLATION.
PubMed=1556067 [NCBI, ExPASy, EBI, Israel, Japan]
Mitchell C., Morris P.W., Vary J.C.;
"Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis.";
J. Bacteriol. 174:2474-2477(1992).
[6]
SIMILARITY TO E.COLI NADE.
PubMed=2118513 [NCBI, ExPASy, EBI, Israel, Japan]
Albertini A.M., Galizzi A.;
"The Bacillus subtilis outB gene is highly homologous to an Escherichia coli ntr-like gene.";
J. Bacteriol. 172:5482-5485(1990).
[7]
CHARACTERIZATION.
DOI=10.1074/jbc.270.11.6181; PubMed=7890752 [NCBI, ExPASy, EBI, Israel, Japan]
Nessi C., Albertini A.M., Speranza M.L., Galizzi A.;
"The outB gene of Bacillus subtilis codes for NAD synthetase.";
J. Biol. Chem. 270:6181-6185(1995).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=8895556 [NCBI, ExPASy, EBI, Israel, Japan]
Rizzi M., Nessi C., Mattevi A., Coda A., Bolognesi M., Galizzi A.;
"Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis.";
EMBO J. 15:5125-5134(1996).
[9]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
DOI=10.1016/S0969-2126(98)00114-2; PubMed=9753692 [NCBI, ExPASy, EBI, Israel, Japan]
Rizzi M., Bolognesi M., Coda A.;
"A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate intermediate in the NAD+ synthetase structure.";
Structure 6:1129-1140(1998).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATES.
DOI=10.1107/S0907444901003523; PubMed=11375500 [NCBI, ExPASy, EBI, Israel, Japan]
Devedjiev Y., Symersky J., Singh R., Jedrzejas M., Brouillette C., Brouillette W., Muccio D., Chattopadhyay D., DeLucas L.;
"Stabilization of active-site loops in NH3-dependent NAD+ synthetase from Bacillus subtilis.";
Acta Crystallogr. D 57:806-812(2001).
[11]
X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATES.
DOI=10.1107/S0907444902006698; PubMed=12077433 [NCBI, ExPASy, EBI, Israel, Japan]
Symersky J., Devedjiev Y., Moore K., Brouillette C., DeLucas L.;
"NH3-dependent NAD+ synthetase from Bacillus subtilis at 1 A resolution.";
Acta Crystallogr. D 58:1138-1146(2002).
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
M15811; AAA22635.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D50453; BAA08947.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99105; CAB12107.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A26936; A26936.
RefSeq NP_388195.1; -.
3D structure databases
PDB
1EE1; X-ray; 2.06 A; A/B=1-272.[ExPASy / RCSB / EBI]
1FYD; X-ray; 2.25 A; A/B=1-272.[ExPASy / RCSB / EBI]
1IFX; X-ray; 2.25 A; A/B=1-272.[ExPASy / RCSB / EBI]
1IH8; X-ray; 1.90 A; A/B=1-272.[ExPASy / RCSB / EBI]
1KQP; X-ray; 1.03 A; A/B=1-272.[ExPASy / RCSB / EBI]
1NSY; X-ray; 2.00 A; A/B=1-272.[ExPASy / RCSB / EBI]
2NSY; X-ray; 2.00 A; A/B=1-272.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EE1; -.
1FYD; -.
1IFX; -.
1IH8; -.
1KQP; -.
1NSY; -.
2NSY; -.
ModBase P08164.
Enzyme and pathway databases
BioCyc BSUB224308:BSU0314-MON; -.
Organism-specific databases
SubtiList BG10694; nadE. [Micado]
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0008795; Molecular function: NAD+ synthase activity (inferred from electronic annotation from EC).
GO:0009435; Biological process: NAD biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0006950; Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
GO:0030435; Biological process: sporulation resulting in formation of a cellular spore (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00193; -; 1.
PBIL [Tree]
InterPro IPR003694; NAD_synthase.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
Pfam PF02540; NAD_synthase; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00552; nadE; 1.
BLOCKS P08164.
ProtoNet P08164.
Genome annotation databases
GeneID 938339; -.
GenomeReviews AL009126_GR; BSU03130.
KEGG bsu:BSU03130; -.
NMPDR fig|224308.1.peg.314; -.
Phylogenomic databases
HOGENOM P08164; -.
Other
DrugBank DB00131; Adenosine monophosphate.
LinkHub P08164; -.
Genome annotation databases
CMR P08164; BSU03130.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; NAD; Nucleotide-binding; Phosphoprotein; Sporulation; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   272  271     NH(3)-dependent NAD(+) synthetase. PRO_0000152159
NP_BIND   45    52  8     ATP. 
NP_BIND   168   178  11     NAD. 
BINDING   33    33        NAD. 
BINDING   79    79        ATP. 
BINDING   85    85        ATP. 
BINDING   138   138        NAD. 
BINDING   158   158        ATP. 
BINDING   209   209        ATP. 
BINDING   224   224        NAD. 
BINDING   259   259        NAD. 
HELIX   3    11  9      
HELIX   19    37  19      
STRAND   41    45  5      
HELIX   50    68  19      
STRAND   74    79  6      
STRAND   82    84  3      
HELIX   88    98  11      
STRAND   101   105  5      
HELIX   109   123  15      
HELIX   129   151  23      
STRAND   154   156  3      
HELIX   161   164  4      
TURN   165   167  3      
TURN   171   175  5      
TURN   181   184  4      
HELIX   187   196  10      
HELIX   202   205  4      
STRAND   214   216  3      
HELIX   221   225  5      
HELIX   229   236  8      
HELIX   243   255  13      
HELIX   257   260  4      
Sequence information
Length: 272 AA [This is the length of the unprocessed precursor] Molecular weight: 30395 Da [This is the MW of the unprocessed precursor] CRC64: 8021E88B5946C2E0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSMQEKIMRE LHVKPSIDPK QEIEDRVNFL KQYVKKTGAK GFVLGISGGQ DSTLAGRLAQ 

        70         80         90        100        110        120 
LAVESIREEG GDAQFIAVRL PHGTQQDEDD AQLALKFIKP DKSWKFDIKS TVSAFSDQYQ 

       130        140        150        160        170        180 
QETGDQLTDF NKGNVKARTR MIAQYAIGGQ EGLLVLGTDH AAEAVTGFFT KYGDGGADLL 

       190        200        210        220        230        240 
PLTGLTKRQG RTLLKELGAP ERLYLKEPTA DLLDEKPQQS DETELGISYD EIDDYLEGKE 

       250        260        270 
VSAKVSEALE KRYSMTEHKR QVPASMFDDW WK 

P08164 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 ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!