Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q2T559

- ASPD_BURTA

UniProt

Q2T559 - ASPD_BURTA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
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 sitei128 – 1281NAD; 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

BioCyciBTHA271848:GJMY-4837-MONOMER.
UniPathwayiUPA00253; UER00456.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable L-aspartate dehydrogenaseUniRule annotation (EC:1.4.1.21UniRule annotation)
Gene namesi
Name:nadXUniRule annotation
Ordered Locus Names:BTH_II1494
OrganismiBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Taxonomic identifieri271848 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000001930: Chromosome II

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Probable L-aspartate dehydrogenasePRO_1000067301Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi271848.BTH_II1494.

Structurei

3D structure databases

ProteinModelPortaliQ2T559.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1712.
HOGENOMiHOG000206326.
KOiK06989.
OMAiECAGHSA.
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.

Q2T559-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRNAHAPVDV AMIGFGAIGA AVYRAVEHDA ALRVAHVIVP EHQCDAVRGA
60 70 80 90 100
LGERVDVVSS VDALAYRPQF ALECAGHGAL VDHVVPLLRA GTDCAVASIG
110 120 130 140 150
ALSDLALLDA LSEAADEGGA TLTLLSGAIG GVDALAAAKQ GGLDEVQYIG
160 170 180 190 200
RKPPLGWLGT PAEALCDLRA MTAEQTIFEG SARDAARLYP KNANVAATVA
210 220 230 240 250
LAGVGLDATK VRLIADPAVT RNVHRVVARG AFGEMSIEMS GKPLPDNPKT
260 270
SALTAFSAIR ALRNRASHCV I
Length:271
Mass (Da):27,879
Last modified:January 24, 2006 - v1
Checksum:i31A11B4983DF4AD8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000085 Genomic DNA. Translation: ABC35596.1.
RefSeqiYP_439690.1. NC_007650.1.

Genome annotation databases

EnsemblBacteriaiABC35596; ABC35596; BTH_II1494.
GeneIDi3844889.
KEGGibte:BTH_II1494.
PATRICi19300644. VBIBurTha36512_1651.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000085 Genomic DNA. Translation: ABC35596.1 .
RefSeqi YP_439690.1. NC_007650.1.

3D structure databases

ProteinModelPortali Q2T559.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 271848.BTH_II1494.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC35596 ; ABC35596 ; BTH_II1494 .
GeneIDi 3844889.
KEGGi bte:BTH_II1494.
PATRICi 19300644. VBIBurTha36512_1651.

Phylogenomic databases

eggNOGi COG1712.
HOGENOMi HOG000206326.
KOi K06989.
OMAi ECAGHSA.
OrthoDBi EOG6ND0JC.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci BTHA271848:GJMY-4837-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. "Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
    Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
    BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Entry informationi

Entry nameiASPD_BURTA
AccessioniPrimary (citable) accession number: Q2T559
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 24, 2006
Last modified: October 1, 2014
This is version 58 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