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 Q8TS47


[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_METAC
Primary accession number Q8TS47
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on June 1, 2002 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 39)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: MA_0958
From
Methanosarcina acetivorans [TaxID: 2214] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
DOI=10.1101/gr.223902; PubMed=11932238 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.;
"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.";
Genome Res. 12:532-542(2002).
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
AE010299; AAM04391.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_615911.1; -.
3D structure databases
HSSP Q9X1X6; 1J5P. [HSSP ENTRY / PDB]
ModBase Q8TS47.
Enzyme and pathway databases
BioCyc MACE188937:MA0958-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 Q8TS47.
Genome annotation databases
GeneID 1472848; -.
GenomeReviews AE010299_GR; MA_0958.
KEGG mac:MA0958; -.
NMPDR fig|188937.1.peg.937; -.
Phylogenomic databases
HOGENOM Q8TS47; -.
Genome annotation databases
CMR Q8TS47; MA_0958.
Other
ProtoNet Q8TS47.
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_0000144895
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: 28578 Da [This is the MW of the unprocessed precursor] CRC64: 06D17290784BBBDA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLKIGIVGCG FIGGQICRAI DGGEVSAELY ALCDSSESKA LELAASLKTC KPSYMKIEEL 

        70         80         90        100        110        120 
IRGVDLIIES ASQNAVRFIV PQALKAGCDV MILSVGALAD EELRDTLFGL AKEHNCKLYF 

       130        140        150        160        170        180 
PSGAVVGIDG LNSASAAGIS SVTLSTRKPP AGLMGAPYVV EHGIELEKLE KKTVLFEGPA 

       190        200        210        220        230        240 
SEAVKAFPAN VNVAATISLA GIGFERTRVK VIADPSLFRN VHEIIVEGEF GKFSTRVENL 

       250        260        270 
PSPENPKTSY LAALSAVSTL KKILNPVQIG T 

Q8TS47 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!