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Q8PV99 (ASPD_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable L-aspartate dehydrogenase
EC=1.4.1.21
Gene names
Name:nadX
Ordered Locus Names:MM_2072
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate By similarity. HAMAP MF_01265

Catalytic activity

L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H. HAMAP MF_01265

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. HAMAP MF_01265

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia By similarity. HAMAP MF_01265

Sequence similarities

Belongs to the L-aspartate dehydrogenase family.

Sequence caution

The sequence AAM31768.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

NADP catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

aspartate dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Probable L-aspartate dehydrogenase HAMAP MF_01265
PRO_0000144898

Sites

Active site2221 By similarity
Binding site1241NAD; via amide nitrogen By similarity
Binding site1921NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8PV99 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: 466E329688C58EC3

FASTA27128,615
        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

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
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. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE008384 Genomic DNA. Translation: AAM31768.1. Different initiation.
RefSeqNP_634096.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ8PV99.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1480414.
GenomeReviewsGene locus MM_2072 in contig AE008384_GR.
KEGGmma:MM_2072.
NMPDRfig|192952.1.peg.2072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649642.
OMAECAGHSA.

Enzyme and pathway databases

BioCycMMAZ192952:MM2072-MONOMER.

Family and domain databases

HAMAPMF_01265. NadX.
[Tree]
InterProIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR011182. Asp_DH_NAD_syn.
IPR020626. Asp_DH_NAD_syn_prok.
IPR022487. Asp_DH_NAD_synth_arc.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK06989.
PfamPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF005227. Asp_dh_NAD_syn. 1 hit.
TIGRFAMsTIGR03855. NAD_NadX. 1 hit.
ProtoNetSearch...

Entry information

Entry nameASPD_METMA
AccessionPrimary (citable) accession number: Q8PV99
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: November 16, 2011
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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