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UniProtKB/Swiss-Prot entry Q7VX83

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

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Entry information
Entry name ASPD2_BORPE
Primary accession number Q7VX83
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 34)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase 2
Synonym EC 1.4.1.21
Gene name
Name: nadX2
OrderedLocusNames: BP1922
From
Bordetella pertussis [TaxID: 520] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Alcaligenaceae; Bordetella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
DOI=10.1038/ng1227; PubMed=12910271 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(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
BX640416; CAE42204.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_880608.1; -.
3D structure databases
HSSP Q9X1X6; 1J5P. [HSSP ENTRY / PDB]
ModBase Q7VX83.
Enzyme and pathway databases
BioCyc BPER257313:BP1922-MON; -.
Ontologies
GO
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from HAMAP).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from HAMAP).
GO:0016639; Molecular function: oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor (inferred from electronic annotation from HAMAP).
GO:0009435; Biological process: NAD biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01265; -; 1.
PBIL [Tree]
InterPro IPR005106; Asp/hSer_DHase_NAD-bd.
IPR002811; Asp_DHase.
IPR011182; Asp_DHase_NAD_syn.
Graphical view of domain structure.
Pfam PF01958; DUF108; 1.
PF03447; NAD_binding_3; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005227; Asp_dh_NAD_syn; 1.
ProDom PD017325; Asp_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS Q7VX83.
Genome annotation databases
GeneID 2665480; -.
GenomeReviews BX470248_GR; BP1922.
KEGG bpe:BP1922; -.
NMPDR fig|257313.1.peg.1684; -.
Phylogenomic databases
HOGENOM Q7VX83; -.
Genome annotation databases
CMR Q7VX83; BP1922.
Other
ProtoNet Q7VX83.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   267  267     Probable L-aspartate dehydrogenase 2. PRO_0000144886
ACT_SITE   219   219        By similarity. 
BINDING   123   123        NAD; via amide nitrogen (By similarity). 
BINDING   189   189        NAD (By similarity). 
Sequence information
Length: 267 AA [This is the length of the unprocessed precursor] Molecular weight: 27736 Da [This is the MW of the unprocessed precursor] CRC64: B52ACD7FEDE4EB4D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTHRIAFIGL GAIASDVAAG LLADAAQPCQ LAALTRNAAD LPPALAGRVA LLDGLPGLLA 

        70         80         90        100        110        120 
WRPDLVVEAA GQQAIAEHAE GCLTAGLDMI ICSAGALADD ALRARLIAAA EAGGARIRVP 

       130        140        150        160        170        180 
AGAIAGLDYL QAVAGRDDAE VVYESRKPVA AWRAELPGMG IDPDTLAESR TLFSGPAREA 

       190        200        210        220        230        240 
ALRFPKNLNV AATLALAGIG MTRTRVEVVV DPQARGNQHR IQVRSPLGEM QIELVNAPSP 

       250        260 
ANPKTSWLVA HSVLATIRRH LARFTIG
Q7VX83 in FASTA format

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