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Reviewed, UniProtKB/Swiss-Prot Q126F5 (ASPD_POLSJ)

Last modified November 25, 2008. Version 23. 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: Bpro_3686
OrganismPolaromonas sp. (strain JS666 / ATCC BAA-500) [Complete proteome] [HAMAP]
Taxonomic identifier296591 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas

Protein attributes

Sequence length267 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 – 267267Probable L-aspartate dehydrogenase
PRO_1000067310

Sites

Active site2201 By similarity
Binding site1241NAD; via amide nitrogen By similarity
Binding site1901NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q126F5-1 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: F1000ACBA87EB262

FASTA26727,568
        10         20         30         40         50         60 
MLKIAMIGCG AIGASVLELL HGDSDVVVDR VITVPEARDR TEIAVARWAP RARVLEVLAA 

        70         80         90        100        110        120 
DDAPDLVVEC AGHGAIAAHV VPALERGIPC VVTSVGALSA PGMAQLLEQA ARRGKTQVQL 

       130        140        150        160        170        180 
LSGAIGGIDA LAAARVGGLD SVVYTGRKPP MAWKGTPAEA VCDLDSLTVA HCIFDGSAEQ 

       190        200        210        220        230        240 
AAQLYPKNAN VAATLSLAGL GLKRTQVQLF ADPGVSENVH HVAAHGAFGS FELTMRGRPL 

       250        260 
AANPKTSALT VYSVVRALLN RGRALVI 

« Hide

References

[1]"Complete sequence of chromosome of Polaromonas sp. JS666."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000316 Genomic DNA. Translation: ABE45587.1.
RefSeqYP_550485.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4013636.
GenomeReviewsGene locus Bpro_3686 in contig CP000316_GR.
KEGGpol:Bpro_3686.
NMPDRfig|296591.1.peg.1652.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ126F5.

Enzyme and pathway databases

BioCycPSP296591:BPRO_3686-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_POLSJ
AccessionPrimary (citable) accession number: Q126F5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 22, 2006
Last modified: November 25, 2008
This is version 23 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