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UniProtKB/Swiss-Prot entry Q12VF1

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

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Entry information
Entry name ASPD_METBU
Primary accession number Q12VF1
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    November 25, 2008 (Entry version 22)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: Mbur_1681
From
Methanococcoides burtonii (strain DSM 6242) [TaxID: 259564] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanococcoides.
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., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P.;
"Complete sequence of Methanococcoides burtonii DSM 6242.";
Submitted (MAR-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
CP000300; ABE52575.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_566325.1; -.
3D structure databases
ModBase Q12VF1.
Enzyme and pathway databases
BioCyc MBUR259564:MBUR_1681-MON; -.
Ontologies
GO
GO:0033735; Molecular function: aspartate dehydrogenase activity (inferred from electronic annotation from InterPro).
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).
GO:0006742; Biological process: NADP catabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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]
ProtoNet Q12VF1.
Genome annotation databases
GeneID 3998077; -.
GenomeReviews CP000300_GR; Mbur_1681.
KEGG mbu:Mbur_1681; -.
NMPDR fig|259564.8.peg.1603; -.
Phylogenomic databases
HOGENOM Q12VF1; -.
Genome annotation databases
CMR Q12VF1; Mbur_1681.
Other
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_1000067304
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: 29094 Da [This is the MW of the unprocessed precursor] CRC64: 00D97CE0518CAB6A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLKIGVFGCG AIGTELCKAI DSGHIEVELY AVYDRHEQSI INLKEQLKNT DPKVLEIVEM 

        70         80         90        100        110        120 
VKHVDLVVEC ASQQAVYDVV PTTLHAKCDV MVISVGAFAD KKLLDTTFDI AKEYGCKIYF 

       130        140        150        160        170        180 
PSGAIVGLDG LKSASAASIY SVTLTTQKHP RSFEGAPYIV QNNIDLDSIK GKTVLFEGMA 

       190        200        210        220        230        240 
SEAVKAFPSN VNVAASLSIA GIGFDKTKVK IIANPALTRN IHEITVEGEF GMFTTRVENV 

       250        260        270 
PAPSNPKTSY LAALSAISTL KKIADPLQVG T
Q12VF1 in FASTA format

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