ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q58325

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ASPD_METJA
Primary accession number Q58325
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 52)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: MJ0915
From
Methanocaldococcus jannaschii (Methanococcus jannaschii) [TaxID: 2190] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanococci; Methanococcales; Methanocaldococcaceae; Methanocaldococcus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=8688087 [NCBI, ExPASy, EBI, Israel, Japan]
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.";
Science 273:1058-1073(1996).
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
L77117; AAB98920.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C64414; C64414.
RefSeq NP_247910.1; -.
3D structure databases
HSSP Q9X1X6; 1H2H. [HSSP ENTRY / PDB]
ModBase Q58325.
Enzyme and pathway databases
BioCyc MJAN243232:MJ_0915-MON; -.
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 Q58325.
Genome annotation databases
GeneID 1451804; -.
GenomeReviews L77117_GR; MJ0915.
KEGG mja:MJ0915; -.
NMPDR fig|243232.1.peg.947; -.
TIGR MJ0915; -.
Phylogenomic databases
HOGENOM Q58325; -.
Other
ProtoNet Q58325.
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_0000144896
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: 28755 Da [This is the MW of the unprocessed precursor] CRC64: B2C427DFD3AE1A4F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLKIGIVGCG AIGNFITKKV LDGTIKNAKI SAVYDRNFDK AKTLSERTGA KICSSIDDLV 

        70         80         90        100        110        120 
KEDLDLVVEA ASIKAVEEIA EKSLINNKDV LIMSVGALAD KKLFLKLRDL AKTVGRKIYL 

       130        140        150        160        170        180 
PSGAIGGLDA IKALRLGEIE EVVLKTTKPV AALEDALKNL GYKPEDIKNP VIVFEGDVFK 

       190        200        210        220        230        240 
AIKEFPANIN VSVTLSIAAE FPAKVVIVAD PNAKLNKHEL FVKSSIGTLR VCIENVPFEE 

       250        260 
NPRTSALAAY SAVRLIRDLA EPVKVGT
Q58325 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!