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 A6X792


[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 ASPD_OCHA4
Primary accession number A6X792
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on August 21, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 13)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: Oant_4396
From
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168) [TaxID: 439375] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae; Ochrobactrum.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Garcia E., Richardson P.;
"Complete sequence of chromosome 2 of Ochrobactrum anthropi ATCC 49188.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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
CP000759; ABS17096.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001372925.1; -.
3D structure databases
ModBase A6X792.
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 A6X792.
Genome annotation databases
GeneID 5381939; -.
GenomeReviews CP000759_GR; Oant_4396.
KEGG oan:Oant_4396; -.
CMR A6X792; Oant_4396.
Other
ProtoNet A6X792.
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   268  268     Probable L-aspartate dehydrogenase. PRO_1000067309
ACT_SITE   221   221        By similarity. 
BINDING   125   125        NAD; via amide nitrogen (By similarity). 
BINDING   191   191        NAD (By similarity). 
Sequence information
Length: 268 AA [This is the length of the unprocessed precursor] Molecular weight: 27854 Da [This is the MW of the unprocessed precursor] CRC64: 32BA43AEF0CCFC12 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSVSETIVLV GWGAIGKRVA DLLAERKSSV RIGAVAVRDR SASRDRLPAG AVLIENPAEL 

        70         80         90        100        110        120 
AASGASLVVE AAGRPSVLPW GEAALSTGMD FAVSSTSAFV DDALFQRLKD AAAASGAKLI 

       130        140        150        160        170        180 
IPPGALGGID ALSAASRLSI ESVEHRIIKP AKAWAGTQAA QLVPLDEISE ATVFFTDTAR 

       190        200        210        220        230        240 
KAADAFPQNA NVAVITSLAG IGLDRTRVTL VADPAARLNT HEIIAEGDFG RMHLRFENGP 

       250        260 
LATNPKSSEM TALNLVRAIE NRVATTVI 

A6X792 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 kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!