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Q7WE57

- ASPD3_BORBR

UniProt

Q7WE57 - ASPD3_BORBR

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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: 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: 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.
OMAiFHAKIEN.
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:October 1, 2003 - v1
Checksum:i886F834DB20755BD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX640451 Genomic DNA. Translation: CAE35144.1.
RefSeqiNP_891314.1. NC_002927.3.

Genome annotation databases

EnsemblBacteriaiCAE35144; CAE35144; BB4781.
GeneIDi2659376.
KEGGibbr:BB4781.
PATRICi21143052. VBIBorBro124907_4869.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX640451 Genomic DNA. Translation: CAE35144.1 .
RefSeqi NP_891314.1. NC_002927.3.

3D structure databases

ProteinModelPortali Q7WE57.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 257310.BB4781.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE35144 ; CAE35144 ; BB4781 .
GeneIDi 2659376.
KEGGi bbr:BB4781.
PATRICi 21143052. VBIBorBro124907_4869.

Phylogenomic databases

eggNOGi COG1712.
HOGENOMi HOG000206326.
KOi K06989.
OMAi FHAKIEN.
OrthoDBi EOG6VTK2D.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci BBRO257310:BB4781-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_01265. NadX.
InterProi IPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR020626. Asp_DH_prok.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNeti Search...

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: ATCC BAA-588 / NCTC 13252 / RB50.

Entry informationi

Entry nameiASPD3_BORBR
AccessioniPrimary (citable) accession number: Q7WE57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 1, 2003
Last modified: October 1, 2014
This is version 71 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