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Q7WLJ8 (ASPD2_BORBR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable L-aspartate dehydrogenase 2
EC=1.4.1.21
Gene names
Name:nadX2
Ordered Locus Names:BB1747
OrganismBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]
Taxonomic identifier257310 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

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 MF_01265

Catalytic activity

L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H. HAMAP MF_01265

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. HAMAP MF_01265

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia By similarity. HAMAP MF_01265

Sequence similarities

Belongs to the L-aspartate dehydrogenase family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

NADP catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

aspartate dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 267267Probable L-aspartate dehydrogenase 2 HAMAP MF_01265
PRO_0000144881

Sites

Active site2191 By similarity
Binding site1231NAD; via amide nitrogen By similarity
Binding site1891NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7WLJ8 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 319D9BDC4BE4EF04

FASTA26727,810
        10         20         30         40         50         60 
MTHRIAFIGL GAIASDVAAG LLADAAQPCQ LAALTRNAAD LPPALAGRVA LLDGLPGLLA 

        70         80         90        100        110        120 
WRPDLVVEAA GQQAIAEHAE GCLRAGLDMI ICSAGALADD ALRARLIAAA EAGGARIRVP 

       130        140        150        160        170        180 
AGAIAGLDYL QAVAGRDDAE VVYESRKPVA AWRAELPGMG IDPDTLAESR TLFSGPAREA 

       190        200        210        220        230        240 
ALRFPKNLNV AATLALAGIG MTRTRVEVVV DPRARGNQHR IQVRSPLGEM QIELVNAPSP 

       250        260 
ANPKTSWLVA QSVLATIRRH LARFTIG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX640442 Genomic DNA. Translation: CAE32244.1.
RefSeqNP_888292.1. NC_002927.3.

3D structure databases

ProteinModelPortalQ7WLJ8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2662476.
GenomeReviewsGene locus BB1747 in contig BX470250_GR.
KEGGbbr:BB1747.
NMPDRfig|257310.1.peg.1739.
PATRIC21136768. VBIBorBro124907_1768.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649642.
OMALATIRRH.
ProtClustDBPRK13301.

Enzyme and pathway databases

BioCycBBRO257310:BB1747-MONOMER.

Family and domain databases

HAMAPMF_01265. NadX.
[Tree]
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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK06989.
PfamPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNetSearch...

Entry information

Entry nameASPD2_BORBR
AccessionPrimary (citable) accession number: Q7WLJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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