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A9A1F7 (ASPD_NITMS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:Nmar_1240
OrganismNitrosopumilus maritimus (strain SCM1) [Reference proteome] [HAMAP]
Taxonomic identifier436308 [NCBI]
Taxonomic lineageArchaeaThaumarchaeotaNitrosopumilalesNitrosopumilaceaeNitrosopumilus

Protein attributes

Sequence length272 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 272272Probable L-aspartate dehydrogenase HAMAP-Rule MF_01265
PRO_1000140088

Sites

Active site2221 By similarity
Binding site1251NAD; via amide nitrogen By similarity
Binding site1921NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A9A1F7 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 66E9C99CAF4E57D9

FASTA27229,185
        10         20         30         40         50         60 
MKRIALLGCG SMGTQIALAI DSENFPATLT HVYDESKDAS FSLTQKLKNK PEIVENSHLL 

        70         80         90        100        110        120 
SSQPIDIVVE AASQNAVKDV ALSVIQNKKD LMIMSVGALL DESIYDILSD ACNDFKKTIY 

       130        140        150        160        170        180 
LPSGAIAGLD GLKSVKDELE SISITTTKHP RSLKGAKFFE TSDINLDEIT SSTVVYKGTA 

       190        200        210        220        230        240 
KEAVTLFPAN INVAALLSLT GIGSEKTSVT IVADPNTDKN THHIEASGKF GTMTFTIENV 

       250        260        270 
PDSNNPKTSR LAILSAIETL KKYCSDDIQI GT 

« Hide

References

[1]"Complete sequence of Nitrosopumilus maritimus SCM1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Stahl D., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SCM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000866 Genomic DNA. Translation: ABX13136.1.
RefSeqYP_001582574.1. NC_010085.1.

3D structure databases

ProteinModelPortalA9A1F7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436308.Nmar_1240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX13136; ABX13136; Nmar_1240.
GeneID5773947.
KEGGnmr:Nmar_1240.

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHOG000206326.
KOK06989.
OMAECAGHSA.

Enzyme and pathway databases

BioCycNMAR436308:GI3J-1273-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_NITMS
AccessionPrimary (citable) accession number: A9A1F7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 46 of the entry and version 1 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