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UniProtKB/Swiss-Prot entry A6UVA8

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

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Entry information
Entry name ASPD_META3
Primary accession number A6UVA8
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 11)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: Maeo_0848
From
Methanococcus aeolicus (strain Nankai-3 / ATCC BAA-1280) [TaxID: 419665] [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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
"Complete sequence of Methanococcus aeolicus Nankai-3.";
Submitted (JUN-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
CP000743; ABR56430.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001325042.1; -.
3D structure databases
ModBase A6UVA8.
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 A6UVA8.
Genome annotation databases
GeneID 5326330; -.
GenomeReviews CP000743_GR; Maeo_0848.
KEGG mae:Maeo_0848; -.
CMR A6UVA8; Maeo_0848.
Other
ProtoNet A6UVA8.
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   266  266     Probable L-aspartate dehydrogenase. PRO_1000067302
ACT_SITE   217   217        By similarity. 
BINDING   123   123        NAD; via amide nitrogen (By similarity). 
BINDING   189   189        NAD (By similarity). 
Sequence information
Length: 266 AA [This is the length of the unprocessed precursor] Molecular weight: 28532 Da [This is the MW of the unprocessed precursor] CRC64: 27EA3020815A7AAA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLKIGIIGCG TIATMIAKAI NYKKINGTIV ALYDKHNDKS QDLNKLTNAK ICDSIDKLVK 

        70         80         90        100        110        120 
EELDIVIECA SIKSVEEVAT KSLNHKKNVV IMSVGALADK NLFSKLYKIA NDNEKKIFVP 

       130        140        150        160        170        180 
SGAIAGVDAI KTASIGRIDE VSLITTKPVY GLEDALKNKG IDTTNISEPT VVFEGTVFDA 

       190        200        210        220        230        240 
IKEFPQNINV SVVLSIASKI PAKVKIVADP SATSNKHEII VKGSIGTIKT VVENNPCKDN 

       250        260 
PKTSALAAYS VIRLLKDLSE PIIVGT
A6UVA8 in FASTA format

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