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Reviewed, UniProtKB/Swiss-Prot Q2FSK9 (ASPD_METHJ)

Last modified November 25, 2008. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 (strain JF-1 / DSM 864) [Complete proteome] [HAMAP]
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

L-aspartate + H(2)O + NAD(P)(+) = oxaloacetate + NH(3) + NAD(P)H.

Pathway

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

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
PRO_1000067305

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q2FSK9-1 [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].

Cross-references

Sequence databases

CP000254 Genomic DNA. Translation: ABD42058.1.
RefSeqYP_503777.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3923251.
GenomeReviewsGene locus Mhun_2354 in contig CP000254_GR.
KEGGmhu:Mhun_2354.
NMPDRfig|323259.5.peg.2478.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2FSK9.

Enzyme and pathway databases

BioCycMHUN323259:MHUN_2354-MON.

Family and domain databases

HAMAPMF_01265.
[Tree]
InterProIPR005106. Asp/hSer_DHase_NAD-bd.
IPR002811. Asp_DHase.
IPR011182. Asp_DHase_NAD_syn.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProDomPD017325. Asp_dh. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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: November 25, 2008
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents