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UniProtKB/Swiss-Prot entry Q8TZ45

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

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Entry information
Entry name ASPD_METKA
Primary accession number Q8TZ45
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 37)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: MK0094
From
Methanopyrus kandleri [TaxID: 2320] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae; Methanopyrus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
DOI=10.1073/pnas.032671499; PubMed=11930014 [NCBI, ExPASy, EBI, Israel, Japan]
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.;
"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.";
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(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
AE010309; AAM01311.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_613381.1; -.
3D structure databases
HSSP Q9X1X6; 1H2H. [HSSP ENTRY / PDB]
ModBase Q8TZ45.
Enzyme and pathway databases
BioCyc MKAN190192:MK0094-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.
Graphical view of domain structure.
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 Q8TZ45.
Genome annotation databases
GeneID 1477397; -.
GenomeReviews AE009439_GR; MK0094.
KEGG mka:MK0094; -.
NMPDR fig|190192.1.peg.94; -.
Phylogenomic databases
HOGENOM Q8TZ45; -.
Genome annotation databases
CMR Q8TZ45; MK0094.
Other
ProtoNet Q8TZ45.
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   262  262     Probable L-aspartate dehydrogenase. PRO_0000144897
ACT_SITE   213   213        By similarity. 
BINDING   128   128        NAD; via amide nitrogen (By similarity). 
BINDING   183   183        NAD (By similarity). 
Sequence information
Length: 262 AA [This is the length of the unprocessed precursor] Molecular weight: 28185 Da [This is the MW of the unprocessed precursor] CRC64: 298438D77FC7BD75 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKKLSLALVG AGGIGTTVLR EIREGRLEGK VEPVLVCDRH PEKLKRIERW FPDCDTSTDL 

        70         80         90        100        110        120 
DDAMSAEADV LLEAASVEAA ASLLPDALKR FDVIVMSVGA LVLEEGLLSR CREVAEVTGH 

       130        140        150        160        170        180 
RLHVPSGAVG GLDVLRALRG RVREVTLTTI KPPKALNKDV SERTVLYEGS VRDAVRKFPK 

       190        200        210        220        230        240 
NINVAAAVSL AVGDPSLVTV RIVCDPEVSV NTHVIEVESS AGTYRFELRN EALPDNPKTS 

       250        260 
AVAAYSAVAL IERMTEGIRV GT
Q8TZ45 in FASTA format

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