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UniProtKB/Swiss-Prot entry Q62BI3

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

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Entry information
Entry name ASPD_BURMA
Primary accession number Q62BI3
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on October 25, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 28)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: BMAA1329
From
Burkholderia mallei (Pseudomonas mallei) [TaxID: 13373] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 23344;
DOI=10.1073/pnas.0403306101; PubMed=15377793 [NCBI, ExPASy, EBI, Israel, Japan]
Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E., Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
"Structural flexibility in the Burkholderia mallei genome.";
Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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
CP000011; AAU46671.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_105945.1; -.
3D structure databases
ModBase Q62BI3.
Enzyme and pathway databases
BioCyc BMAL243160:BMA_A1329-MON; -.
Ontologies
GO
GO:0033735; Molecular function: aspartate dehydrogenase activity (inferred from electronic annotation from EC).
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 Q62BI3.
Genome annotation databases
GeneID 3087458; -.
GenomeReviews CP000011_GR; BMAA1329.
KEGG bma:BMAA1329; -.
TIGR BMAA1329; -.
Phylogenomic databases
HOGENOM Q62BI3; -.
Other
ProtoNet Q62BI3.
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   271  271     Probable L-aspartate dehydrogenase. PRO_0000144888
ACT_SITE   224   224        By similarity. 
BINDING   128   128        NAD; via amide nitrogen (By similarity). 
BINDING   194   194        NAD (By similarity). 
Sequence information
Length: 271 AA [This is the length of the unprocessed precursor] Molecular weight: 27747 Da [This is the MW of the unprocessed precursor] CRC64: 5703F6D14871D311 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRNAHAPVDV AMIGFGAIGA AVYRAVEHDA ALRVAHVIVP EHQCDAVRGA LGERVDVVSS 

        70         80         90        100        110        120 
VDALACRPQF ALECAGHGAL VDHVVPLLKA GTDCAVASIG ALSDLALLDA LSNAADAGGA 

       130        140        150        160        170        180 
TLTLLSGAIG GIDALAAARQ GGLDEVRYIG RKPPLGWLGT PAEAICDLRA MAAEQTIFEG 

       190        200        210        220        230        240 
SARDAAQLYP RNANVAATVA LAGVGLDATR VCLIADPAVT RNVHRIVARG AFGEMSIEMS 

       250        260        270 
GKPLPDNPKT SALTAFSAIR ALRNRASHCV I
Q62BI3 in FASTA format

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