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UniProtKB/Swiss-Prot entry Q8K9W7

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

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Entry information
Entry name NADE_BUCAP
Primary accession number Q8K9W7
Secondary accession numbers None
Integrated into Swiss-Prot on November 15, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 38)
Name and origin of the protein
Protein name NH(3)-dependent NAD(+) synthetase
Synonym EC 6.3.1.5
Gene name
Name: nadE
OrderedLocusNames: BUsg_168
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(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
AE013218; AAM67735.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660524.1; -.
3D structure databases
HSSP P08164; 1KQP. [HSSP ENTRY / PDB]
ModBase Q8K9W7.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG168-MON; -.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0003952; Molecular function: NAD+ synthase (glutamine-hydrolyzing) activity (inferred from electronic annotation from InterPro).
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).
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.
Genome annotation databases
GeneID 1005365; -.
GenomeReviews AE013218_GR; BUsg_168.
KEGG bas:BUsg168; -.
Phylogenomic databases
HOGENOM Q8K9W7; -.
Genome annotation databases
CMR Q8K9W7; BUsg_168.
Other
ProtoNet Q8K9W7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   268  268     NH(3)-dependent NAD(+) synthetase. PRO_0000152161
NP_BIND   46    53  8     ATP (By similarity). 
ACT_SITE   48    48        By similarity. 
Sequence information
Length: 268 AA [This is the length of the unprocessed precursor] Molecular weight: 30605 Da [This is the MW of the unprocessed precursor] CRC64: 0C81021081F88846 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTLQKKIIEL LGVKPLIIPK KEIENRIQIL KRYLIENTHL KTLIVGISGG QDSTLTGKLC 

        70         80         90        100        110        120 
QLSIQELRKE KKEKSYQFIA LRLPYGVQID EKDCRDAINF INPDQIFTIN IKNAVLNSER 

       130        140        150        160        170        180 
SLKKQGIQIS DYIKGNEKAR ERMKVQYSFA AITNGLVVGT GNAAENVTGF FTKYGDNGTD 

       190        200        210        220        230        240 
VNLISKLNKR QGKFLLKELN CPKHLYLKKP TADLEDEKPQ KEDEVALGIK YNIIDDYLEG 

       250        260 
KKVNSLNKQI IERLYLTTEH KRKIINLG
Q8K9W7 in FASTA format

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