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A3MD35

- ASPD_BURM7

UniProt

A3MD35 - ASPD_BURM7

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Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Burkholderia mallei (strain NCTC 10247)
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

BioCyciBMAL320389:GH97-4510-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:BMA10247_A0979
OrganismiBurkholderia mallei (strain NCTC 10247)
Taxonomic identifieri320389 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000002284: Chromosome II

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Probable L-aspartate dehydrogenasePRO_1000067294Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi320389.BMA10247_A0979.

Structurei

3D structure databases

ProteinModelPortaliA3MD35.
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.

A3MD35-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRNAHAPVDV AMIGFGAIGA AVYRAVEHDA ALRVAHVIVP EHQCDAVRGA
60 70 80 90 100
LGERVDVVSS VDALACRPQF ALECAGHGAL VDHVVPLLKA GTDCAVASIG
110 120 130 140 150
ALSDLALLDA LSNAADAGGA TLTLLSGAIG GIDALAAARQ GGLDEVRYIG
160 170 180 190 200
RKPPLGWLGT PAEAICDLRA MAAEQTIFEG SARDAAQLYP RNANVAATVA
210 220 230 240 250
LAGVGLDATR VCLIADPAVT RNVHRIVARG AFGEMSIEMS GKPLPDNPKT
260 270
SALTAFSAIR ALRNRASHCV I
Length:271
Mass (Da):27,747
Last modified:April 3, 2007 - v1
Checksum:i5703F6D14871D311
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000547 Genomic DNA. Translation: ABO03049.1.
RefSeqiYP_001078171.1. NC_009079.1.

Genome annotation databases

EnsemblBacteriaiABO03049; ABO03049; BMA10247_A0979.
GeneIDi4890690.
KEGGibmn:BMA10247_A0979.
PATRICi19139687. VBIBurMal96640_0915.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000547 Genomic DNA. Translation: ABO03049.1 .
RefSeqi YP_001078171.1. NC_009079.1.

3D structure databases

ProteinModelPortali A3MD35.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 320389.BMA10247_A0979.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO03049 ; ABO03049 ; BMA10247_A0979 .
GeneIDi 4890690.
KEGGi bmn:BMA10247_A0979.
PATRICi 19139687. VBIBurMal96640_0915.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci BMAL320389:GH97-4510-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 10247.

Entry informationi

Entry nameiASPD_BURM7
AccessioniPrimary (citable) accession number: A3MD35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 3, 2007
Last modified: October 1, 2014
This is version 53 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