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UniProtKB/Swiss-Prot entry Q8PV99

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

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Entry information
Entry name ASPD_METMA
Primary accession number Q8PV99
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on August 16, 2005 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 41)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: MM_2072
From
Methanosarcina mazei (Methanosarcina frisia) [TaxID: 2209] [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 BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
PubMed=12125824 [NCBI, ExPASy, EBI, Israel, Japan]
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.;
"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.";
J. Mol. Microbiol. Biotechnol. 4:453-461(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
AE008384; AAM31768.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_634096.1; -.
3D structure databases
HSSP Q9X1X6; 1J5P. [HSSP ENTRY / PDB]
ModBase Q8PV99.
Enzyme and pathway databases
BioCyc MMAZ192952:MM2072-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 Q8PV99.
Genome annotation databases
GeneID 1480414; -.
GenomeReviews AE008384_GR; MM_2072.
KEGG mma:MM_2072; -.
NMPDR fig|192952.1.peg.2072; -.
Phylogenomic databases
HOGENOM Q8PV99; -.
Genome annotation databases
CMR Q8PV99; MM_2072.
Other
ProtoNet Q8PV99.
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_0000144898
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: 28615 Da [This is the MW of the unprocessed precursor] CRC64: 466E329688C58EC3 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLKIGIIGCG FIGGQICRAI DSGEIDAELY ALCDSSESKA FGLAKSLNTC KPAYMKIEEL 

        70         80         90        100        110        120 
ISSVDLVVES ASQNAVRFIV PQALKAGCSV MVLSVGALAD KELRETLFGL AKKHNCKLYF 

       130        140        150        160        170        180 
PSGAVVGIDG INSAHAAGIS SVTLTTRKPP SGLMGAPYVV EHGIELEKLE KETILFEGTA 

       190        200        210        220        230        240 
SEAVKAFPAN VNVAATISLA GIGFERTMVR VIADPSLSRN IHEINVEGEF GKFCTKVENL 

       250        260        270 
PSPENPKTSY LAALSAISTL KKILNPVQIG T
Q8PV99 in FASTA format

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