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A2RXI5

- ASPD_BURM9

UniProt

A2RXI5 - ASPD_BURM9

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Protein

Probable L-aspartate dehydrogenase

Gene
nadX, BMA10229_0588
Organism
Burkholderia mallei (strain NCTC 10229)
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 By similarity.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 nitrogen By similarity
Binding sitei194 – 1941NAD By similarity
Active sitei224 – 2241 By similarity

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

BioCyciBMAL412022:GJI8-3996-MONOMER.
UniPathwayiUPA00253; UER00456.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable L-aspartate dehydrogenase (EC:1.4.1.21)
Gene namesi
Name:nadX
Ordered Locus Names:BMA10229_0588
OrganismiBurkholderia mallei (strain NCTC 10229)
Taxonomic identifieri412022 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000002283: Chromosome II

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Probable L-aspartate dehydrogenaseUniRule annotationPRO_1000067295Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi412022.BMA10229_0588.

Structurei

3D structure databases

ProteinModelPortaliA2RXI5.

Family & Domainsi

Sequence similaritiesi

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.

A2RXI5-1 [UniParc]FASTAAdd to Basket

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MRNAHAPVDV AMIGFGAIGA AVYRAVEHDA ALRVAHVIVP EHQCDAVRGA    50
LGERVDVVSS VDALACRPQF ALECAGHGAL VDHVVPLLKA GTDCAVASIG 100
ALSDLALLDA LSNAADAGGA TLTLLSGAIG GIDALAAARQ GGLDEVRYIG 150
RKPPLGWLGT PAEAICDLRA MAAEQTIFEG SARDAAQLYP RNANVAATVA 200
LAGVGLDATR VCLIADPAVT RNVHRIVARG AFGEMSIEMS GKPLPDNPKT 250
SALTAFSAIR ALRNRASHCV I 271
Length:271
Mass (Da):27,747
Last modified:March 6, 2007 - v1
Checksum:i5703F6D14871D311
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000545 Genomic DNA. Translation: ABM98587.1.
RefSeqiYP_001024404.1. NC_008835.1.

Genome annotation databases

EnsemblBacteriaiABM98587; ABM98587; BMA10229_0588.
GeneIDi4789326.
KEGGibml:BMA10229_0588.
PATRICi19127695. VBIBurMal46188_0580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000545 Genomic DNA. Translation: ABM98587.1 .
RefSeqi YP_001024404.1. NC_008835.1.

3D structure databases

ProteinModelPortali A2RXI5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 412022.BMA10229_0588.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM98587 ; ABM98587 ; BMA10229_0588 .
GeneIDi 4789326.
KEGGi bml:BMA10229_0588.
PATRICi 19127695. VBIBurMal46188_0580.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci BMAL412022:GJI8-3996-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. DeShazer D., Woods D.E., Nierman W.C.
    Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 10229.

Entry informationi

Entry nameiASPD_BURM9
AccessioniPrimary (citable) accession number: A2RXI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 6, 2007
Last modified: September 3, 2014
This is version 51 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 By similarity.

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

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