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Q2FSK9 (ASPD_METHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:Mhun_2354
OrganismMethanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) [Reference proteome] [HAMAP]
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

Protein attributes

Sequence length252 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 – 252252Probable L-aspartate dehydrogenase HAMAP-Rule MF_01265
PRO_1000067305

Sites

Active site2031 By similarity
Binding site1191NAD; via amide nitrogen By similarity
Binding site1751NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2FSK9 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: DB0A2E0F122E4710

FASTA25227,227
        10         20         30         40         50         60 
MVRIGLLGCG NVGRIIATHQ DGFTVEALFD RLPDHAEELA RMCGAPAYAD FQEFISQDFD 

        70         80         90        100        110        120 
ICVEAASVLA VREYAPKILE NGKHVLILSV GALSDTNFRK ILLDVARSQG KKIHIPSGAI 

       130        140        150        160        170        180 
MGLDNLKVGG ISRIDSVLLR TTKSPASLGM QVSHRTLAFR GKANECIKQF PKNINVSVAL 

       190        200        210        220        230        240 
ALAVHHDVDV ELWADPEVDR NIHDIFVSGE FGEASIRVVN HPSPDNPATS YLAALSVLSL 

       250 
LKNLDSPLVI GS 

« Hide

References

[1]"Complete sequence of Methanospirillum hungatei JF-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27890 / DSM 864 / NBRC 100397 / JF-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000254 Genomic DNA. Translation: ABD42058.1.
RefSeqYP_503777.1. NC_007796.1.

3D structure databases

ProteinModelPortalQ2FSK9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323259.Mhun_2354.

Proteomic databases

PRIDEQ2FSK9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD42058; ABD42058; Mhun_2354.
GeneID3923251.
KEGGmhu:Mhun_2354.

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHOG000206326.
KOK06989.
OMAECAGHSA.

Enzyme and pathway databases

BioCycMHUN323259:GH0L-2385-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_METHJ
AccessionPrimary (citable) accession number: Q2FSK9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 21, 2006
Last modified: May 14, 2014
This is version 53 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