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UniProtKB/Swiss-Prot entry A4FY69

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

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Entry information
Entry name ASPD_METM5
Primary accession number A4FY69
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on April 17, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 14)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: MmarC5_0845
From
Methanococcus maripaludis (strain C5 / ATCC BAA-1333) [TaxID: 402880] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanococci; Methanococcales; Methanococcaceae; Methanococcus.
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., Chertkov O., Brettin T., Bruce D., Han C., Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
"Complete sequence of chromosome of Methanococcus maripaludis C5.";
Submitted (MAR-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
CP000609; ABO35153.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001097368.1; -.
3D structure databases
ModBase A4FY69.
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.
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 A4FY69.
Genome annotation databases
GeneID 4929041; -.
GenomeReviews CP000609_GR; MmarC5_0845.
KEGG mmq:MmarC5_0845; -.
CMR A4FY69; MmarC5_0845.
Other
ProtoNet A4FY69.
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_1000067306
ACT_SITE   218   218        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: 28716 Da [This is the MW of the unprocessed precursor] CRC64: F8CCA8263E10E6D1 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLKVGVVGCG AIASLITKAL MSDRLNKAEV LAFYDGNLEK AEKLAMETGA DFCRSLDELV 

        70         80         90        100        110        120 
SKDLDLIVEC ASVTAVEDTV IKSLNNGKDV IIMSVGAFAD KDLFLKLYKL AEKLERKIYI 

       130        140        150        160        170        180 
PSGAVAGIDA VKSGSLGKIS DVTLTTTKPV HGLKNALEEQ GLNTDEIKEP KTVFEGTVFE 

       190        200        210        220        230        240 
AISKFPQNIN VSVVLSLASR YPAKVKIIAD PCAVVNRHEI FVKGSIGTIK TCVENNPCRD 

       250        260 
NPKTSALAAY SVIRLIKDLS EPIRIGT
A4FY69 in FASTA format

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