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B3R8S4

- ASPD_CUPTR

UniProt

B3R8S4 - ASPD_CUPTR

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Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Cupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424))
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 sitei123 – 1231NAD; via amide nitrogenUniRule annotation
Binding sitei189 – 1891NADUniRule annotation
Active sitei219 – 2191UniRule 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

BioCyciCTAI164546:GJNE-3784-MONOMER.
CTAI977880:GLC7-3784-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:RALTA_B0572
OrganismiCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424))
Taxonomic identifieri164546 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000001692: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Probable L-aspartate dehydrogenasePRO_1000140086Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi164546.RALTA_B0572.

Structurei

3D structure databases

ProteinModelPortaliB3R8S4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1712.
HOGENOMiHOG000206326.
KOiK06989.
OMAiRARGNQH.
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.

B3R8S4 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLHVSMVGCG AIGRGVLELL KSDPDVVFDV VIVPEHTMDE ARGAVSALAP
60 70 80 90 100
RARVATHLDD QRPDLLVECA GHHALEEHIV PALERGIPCM VVSVGALSEP
110 120 130 140 150
GMAERLEAAA RRGGTQVQLL SGAIGAIDAL AAARVGGLDE VIYTGRKPAR
160 170 180 190 200
AWTGTPAEQL FDLEALTEAT VIFEGTARDA ARLYPKNANV AATVSLAGLG
210 220 230 240 250
LDRTAVKLLA DPHAVENVHH VEARGAFGGF ELTMRGKPLA ANPKTSALTV
260
FSVVRALGNR AHAVSI
Length:266
Mass (Da):27,799
Last modified:September 2, 2008 - v1
Checksum:iACE91AE7E3C72B96
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU633750 Genomic DNA. Translation: CAQ71192.1.
RefSeqiYP_002007253.1. NC_010530.1.

Genome annotation databases

EnsemblBacteriaiCAQ71192; CAQ71192; RALTA_B0572.
GeneIDi6455299.
KEGGicti:RALTA_B0572.
PATRICi21534923. VBICupTai42494_4076.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU633750 Genomic DNA. Translation: CAQ71192.1 .
RefSeqi YP_002007253.1. NC_010530.1.

3D structure databases

ProteinModelPortali B3R8S4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 164546.RALTA_B0572.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAQ71192 ; CAQ71192 ; RALTA_B0572 .
GeneIDi 6455299.
KEGGi cti:RALTA_B0572.
PATRICi 21534923. VBICupTai42494_4076.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci CTAI164546:GJNE-3784-MONOMER.
CTAI977880:GLC7-3784-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: R1 / LMG 19424.

Entry informationi

Entry nameiASPD_CUPTR
AccessioniPrimary (citable) accession number: B3R8S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: October 1, 2014
This is version 44 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