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UniProtKB/Swiss-Prot entry Q46BD6

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

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Entry information
Entry name ASPD_METBF
Primary accession number Q46BD6
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on September 13, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 21)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: Mbar_A1866
From
Methanosarcina barkeri (strain Fusaro / DSM 804) [TaxID: 269797] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.00810-06; PubMed=16980466 [NCBI, ExPASy, EBI, Israel, Japan]
Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.";
J. Bacteriol. 188:7922-7931(2006).
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
CP000099; AAZ70806.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_305386.1; -.
3D structure databases
ModBase Q46BD6.
Enzyme and pathway databases
BioCyc MBAR269797:MBAR_A1866-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 Q46BD6.
Genome annotation databases
GeneID 3624568; -.
GenomeReviews CP000099_GR; Mbar_A1866.
KEGG mba:Mbar_A1866; -.
NMPDR fig|269797.3.peg.2965; -.
Phylogenomic databases
HOGENOM Q46BD6; -.
Genome annotation databases
CMR Q46BD6; Mbar_A1866.
Other
ProtoNet Q46BD6.
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_1000067303
ACT_SITE   222   222        By similarity. 
BINDING   124   124        NAD; via amide nitrogen (By similarity). 
BINDING   192   192        NAD (By similarity). 
Sequence information
Length: 271 AA [This is the length of the unprocessed precursor] Molecular weight: 28823 Da [This is the MW of the unprocessed precursor] CRC64: 868F364A30900982 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLKIGVIGCG FIGGQICRAI DKGVINAELY ALSDSSESKV LELTTCLKRY SPASMTIEEL 

        70         80         90        100        110        120 
LQNVDFVIES ASQKAVRLIV PQALEAGRDV MVMSVGALAD EELRKRLFRL AEQNNCKLYF 

       130        140        150        160        170        180 
PSGAVAGIDG INSASAAEIL SVTLTTRKPP MGLAGAPHVE ALGIELETIE KETLLFEGPA 

       190        200        210        220        230        240 
SEAVKAFPAN VNVAATISLA GIGFERTKVR VIADPTLSRN VHEITVEGEF GKLSTRVENL 

       250        260        270 
PSPENPKTSY LAALSAISTL KKILSPVQIG T
Q46BD6 in FASTA format

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