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UniProtKB/Swiss-Prot entry Q9PPB0

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

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Entry information
Entry name NADE_CAMJE
Primary accession number Q9PPB0
Secondary accession number Q0PA80
Integrated into Swiss-Prot on November 15, 2002
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 41)
Name and origin of the protein
Protein name NH(3)-dependent NAD(+) synthetase
Synonym EC 6.3.1.5
Gene name
Name: nadE
OrderedLocusNames: Cj0810
From
Campylobacter jejuni [TaxID: 197] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 11168 / Serotype O:2;
DOI=10.1038/35001088; PubMed=10688204 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences.";
Nature 403:665-668(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
AL111168; CAL34938.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B81353; B81353.
3D structure databases
HSSP P08164; 1IH8. [HSSP ENTRY / PDB]
ModBase Q9PPB0.
Protein-protein interaction databases
IntAct Q9PPB0; -.
Enzyme and pathway databases
BioCyc CJEJ192222:CJ0810-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:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
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.
ProtoNet Q9PPB0.
Genome annotation databases
GenomeReviews AL111168_GR; Cj0810.
KEGG cje:Cj0810; -.
CMR Q9PPB0; Cj0810.
Other
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   246  246     NH(3)-dependent NAD(+) synthetase. PRO_0000152162
NP_BIND   29    36  8     ATP (By similarity). 
ACT_SITE   31    31        By similarity. 
Sequence information
Length: 246 AA [This is the length of the unprocessed precursor] Molecular weight: 27463 Da [This is the MW of the unprocessed precursor] CRC64: A92C822F968078EA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDWQKITEKM CDFIQEKVKN SQSQGVVLGL SGGIDSALVA TLCKRALKEN VFALLMPTQI 

        70         80         90        100        110        120 
SNKANLEDAL RLCADLNLEY KIIEIQSILD AFIKQSENTT LVSLGNFAAR IRMSLLYDYS 

       130        140        150        160        170        180 
ALKNSLVIGT SNKSELLLGY GTIYGDLACA FNPIGSLYKS EIYALAKYLN LHENFIKKAP 

       190        200        210        220        230        240 
SADLWENQSD EADLGFSYTK IDEGLKALET NDEKLLRTLD PSLIAMLKNR MQKNAFKGKM 


PEILEI
Q9PPB0 in FASTA format

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