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Q8PV99 (ASPD_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

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-Rule MF_01265

Catalytic activity

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

Pathway

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

Miscellaneous

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

Sequence similarities

Belongs to the L-aspartate dehydrogenase family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Probable L-aspartate dehydrogenase HAMAP-Rule 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

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...
MobiDBSearch...

Protein-protein interaction databases

STRING192952.MM_2072.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM31768; AAM31768; MM_2072.
GeneID1480414.
KEGGmma:MM_2072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHOG000206326.
KOK06989.
OMAECAGHSA.

Enzyme and pathway databases

BioCycMMAZ192952:GCK2-2126-MONOMER.
UniPathwayUPA00253; UER00456.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01265. NadX.
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]
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: May 14, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways