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Q126F5 (ASPD_POLSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:Bpro_3686
OrganismPolaromonas sp. (strain JS666 / ATCC BAA-500) [Complete proteome] [HAMAP]
Taxonomic identifier296591 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas

Protein attributes

Sequence length267 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 – 267267Probable L-aspartate dehydrogenase HAMAP-Rule MF_01265
PRO_1000067310

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q126F5 [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."
US DOE Joint Genome Institute
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].
Strain: JS666 / ATCC BAA-500.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000316 Genomic DNA. Translation: ABE45587.1.
RefSeqYP_550485.1. NC_007948.1.

3D structure databases

ProteinModelPortalQ126F5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING296591.Bpro_3686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE45587; ABE45587; Bpro_3686.
GeneID4013636.
KEGGpol:Bpro_3686.
PATRIC22960604. VBIPolSp102244_3756.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHOG000206326.
KOK06989.
OMAPKTSYLA.
OrthoDBEOG6ND0JC.
ProtClustDBPRK13303.

Enzyme and pathway databases

BioCycPSP296591:GHI4-4405-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.
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.
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: February 19, 2014
This is version 57 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