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Protein

Probable L-aspartate dehydrogenase 2

Gene

nadX2

Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.UniRule annotation

Catalytic activityi

L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H.UniRule annotation

Pathway:iNAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes iminoaspartate from L-aspartate (dehydrogenase route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Probable L-aspartate dehydrogenase 1 (nadX1), Probable L-aspartate dehydrogenase 2 (nadX2)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes iminoaspartate from L-aspartate (dehydrogenase route), the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231NAD; via amide nitrogenUniRule annotation
Binding sitei189 – 1891NADUniRule annotation
Active sitei219 – 2191UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciBPAR257311:BPP2295-MONOMER.
UniPathwayiUPA00253; UER00456.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable L-aspartate dehydrogenase 2UniRule annotation (EC:1.4.1.21UniRule annotation)
Gene namesi
Name:nadX2UniRule annotation
Ordered Locus Names:BPP2295
OrganismiBordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Taxonomic identifieri257311 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001421 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Probable L-aspartate dehydrogenase 2PRO_0000144884Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ7W850.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1712.
HOGENOMiHOG000206326.
KOiK06989.
OMAiRARGNQH.
OrthoDBiEOG6ND0JC.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01265. NadX.
InterProiIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR020626. Asp_DH_prok.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF005227. Asp_dh_NAD_syn. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7W850-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHRIAFIGL GAIASDVAAG LLADAAQPCQ LAALTRNAAD LPPALAGRVA
60 70 80 90 100
LLDGLPGLLA WRPDLVVEAA GQQAIAEHAE GCLKAGLDMI ICSAGALADD
110 120 130 140 150
ALRARLIAAA EAGGARIRVP AGAIAGLDYL QAVAGRDDAE VVYESRKPVA
160 170 180 190 200
AWRAELPGMG IDPDTLAESR TLFSGPAREA ALRFPKNLNV AATLALAGIG
210 220 230 240 250
MTRTRVEVVV DPRARGNQHR IQVRSPLGEM QIELVNAPSP ANPKTSWLVA
260
QSVLATIRRH LARFTIG
Length:267
Mass (Da):27,782
Last modified:October 1, 2003 - v1
Checksum:iF893BCE262E4F60E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640430 Genomic DNA. Translation: CAE37593.1.
RefSeqiWP_010928468.1. NC_002928.3.

Genome annotation databases

EnsemblBacteriaiCAE37593; CAE37593; BPP2295.
KEGGibpa:BPP2295.
PATRICi21148440. VBIBorPar43418_2412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640430 Genomic DNA. Translation: CAE37593.1.
RefSeqiWP_010928468.1. NC_002928.3.

3D structure databases

ProteinModelPortaliQ7W850.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE37593; CAE37593; BPP2295.
KEGGibpa:BPP2295.
PATRICi21148440. VBIBorPar43418_2412.

Phylogenomic databases

eggNOGiCOG1712.
HOGENOMiHOG000206326.
KOiK06989.
OMAiRARGNQH.
OrthoDBiEOG6ND0JC.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00456.
BioCyciBPAR257311:BPP2295-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01265. NadX.
InterProiIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR020626. Asp_DH_prok.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
    Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
    , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
    Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Entry informationi

Entry nameiASPD2_BORPA
AccessioniPrimary (citable) accession number: Q7W850
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 1, 2003
Last modified: July 22, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.UniRule annotation

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.