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UniProtKB/Swiss-Prot entry Q126F5

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

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Entry information
Entry name ASPD_POLSJ
Primary accession number Q126F5
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on August 22, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 20)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: Bpro_3686
From
Polaromonas sp. (strain JS666 / ATCC BAA-500) [TaxID: 296591] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Polaromonas.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Richardson P.;
"Complete sequence of chromosome of Polaromonas sp. JS666.";
Submitted (APR-2006) 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
CP000316; ABE45587.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_550485.1; -.
3D structure databases
ModBase Q126F5.
Enzyme and pathway databases
BioCyc PSP296591:BPRO_3686-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.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
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 Q126F5.
Genome annotation databases
GeneID 4013636; -.
GenomeReviews CP000316_GR; Bpro_3686.
KEGG pol:Bpro_3686; -.
NMPDR fig|296591.1.peg.1652; -.
Phylogenomic databases
HOGENOM Q126F5; -.
Genome annotation databases
CMR Q126F5; Bpro_3686.
Other
ProtoNet Q126F5.
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. PRO_1000067310
ACT_SITE   220   220        By similarity. 
BINDING   124   124        NAD; via amide nitrogen (By similarity). 
BINDING   190   190        NAD (By similarity). 
Sequence information
Length: 267 AA [This is the length of the unprocessed precursor] Molecular weight: 27568 Da [This is the MW of the unprocessed precursor] CRC64: F1000ACBA87EB262 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLKIAMIGCG AIGASVLELL HGDSDVVVDR VITVPEARDR TEIAVARWAP RARVLEVLAA 

        70         80         90        100        110        120 
DDAPDLVVEC AGHGAIAAHV VPALERGIPC VVTSVGALSA PGMAQLLEQA ARRGKTQVQL 

       130        140        150        160        170        180 
LSGAIGGIDA LAAARVGGLD SVVYTGRKPP MAWKGTPAEA VCDLDSLTVA HCIFDGSAEQ 

       190        200        210        220        230        240 
AAQLYPKNAN VAATLSLAGL GLKRTQVQLF ADPGVSENVH HVAAHGAFGS FELTMRGRPL 

       250        260 
AANPKTSALT VYSVVRALLN RGRALVI
Q126F5 in FASTA format

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