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Protein

Probable L-aspartate dehydrogenase 3

Gene

nadX3

Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei126 – 1261NAD; via amide nitrogenUniRule annotation
Binding sitei194 – 1941NADUniRule annotation
Active sitei224 – 2241UniRule annotation

GO - Molecular functioni

  1. aspartate dehydrogenase activity Source: UniProtKB-EC
  2. NAD binding Source: UniProtKB-HAMAP
  3. NADP binding Source: UniProtKB-HAMAP
  4. oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Source: UniProtKB-HAMAP

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-HAMAP
  2. NADP catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciBBRO257310:BB4781-MONOMER.
UniPathwayiUPA00253; UER00456.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable L-aspartate dehydrogenase 3UniRule annotation (EC:1.4.1.21UniRule annotation)
Gene namesi
Name:nadX3UniRule annotation
Ordered Locus Names:BB4781
OrganismiBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Taxonomic identifieri257310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001027 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 272272Probable L-aspartate dehydrogenase 3PRO_0000144882Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi257310.BB4781.

Structurei

3D structure databases

ProteinModelPortaliQ7WE57.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1712.
HOGENOMiHOG000206326.
KOiK06989.
OMAiLEIWADP.
OrthoDBiEOG6VTK2D.

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.

Q7WE57-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSREELGVA VAGLGAIGKA LANRLARNEV AGCRLSAVSG RDPGRTADFI
60 70 80 90 100
ASLPRPVPAV PLHELPRHAD IVVECAPAAV LPQIVEPVLD AGKKVIVLSV
110 120 130 140 150
GALLEFPELF RKAGSSDGQI LVPTGALLGL DAVTAAAEGR IESVKMVSRK
160 170 180 190 200
PPIGFKGAPI LAERNLDIDG LTEPLLLYSG SARAAARGFP ANLNVAVALS
210 220 230 240 250
LAGIGPDETQ LEVWADPGVV RNTHTIEVVS DAALLRMTIE NIPSENPKTG
260 270
RITAQSVMAM LRKMSAPVRV GT
Length:272
Mass (Da):28,270
Last modified:September 30, 2003 - v1
Checksum:i886F834DB20755BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640451 Genomic DNA. Translation: CAE35144.1.
RefSeqiNP_891314.1. NC_002927.3.

Genome annotation databases

KEGGibbr:BB4781.
PATRICi21143052. VBIBorBro124907_4869.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640451 Genomic DNA. Translation: CAE35144.1.
RefSeqiNP_891314.1. NC_002927.3.

3D structure databases

ProteinModelPortaliQ7WE57.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257310.BB4781.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGibbr:BB4781.
PATRICi21143052. VBIBorBro124907_4869.

Phylogenomic databases

eggNOGiCOG1712.
HOGENOMiHOG000206326.
KOiK06989.
OMAiLEIWADP.
OrthoDBiEOG6VTK2D.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00456.
BioCyciBBRO257310:BB4781-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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-588 / NCTC 13252 / RB50.

Entry informationi

Entry nameiASPD3_BORBR
AccessioniPrimary (citable) accession number: Q7WE57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2005
Last sequence update: September 30, 2003
Last modified: March 31, 2015
This is version 73 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.