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A3M394

- ASPD_ACIBT

UniProt

A3M394 - ASPD_ACIBT

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Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755)
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 sitei120 – 1201NAD; via amide nitrogenUniRule annotation
Binding sitei186 – 1861NADUniRule annotation
Active sitei216 – 2161UniRule 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

BioCyciABAU400667:GI0Q-944-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:A1S_0956
OrganismiAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755)
Taxonomic identifieri400667 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex
ProteomesiUP000006737: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Probable L-aspartate dehydrogenasePRO_1000140084Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi400667.A1S_0956.

Structurei

3D structure databases

ProteinModelPortaliA3M394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1712.
HOGENOMiHOG000206326.
KOiK06989.
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.

A3M394-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKLMMIGFG AMAAEVYAHL PQDLQLKWIV VPSRSIEKVQ SQVSSDIQVI
60 70 80 90 100
SDIEQCDGTP DYVIEVAGQA AVKEHAQKVL AKGWTIGLIS VGTLADSEFL
110 120 130 140 150
VQLKQTAEKN DAHLHLLAGA IAGIDGISAA KEGGLQKVTY KGCKSPKSWK
160 170 180 190 200
GSYAEQLVDL DHVSEPTVFF TGTAREAAMK FPANANVAAT IALAGLGMDE
210 220 230 240 250
TMVELTVDPT INKNKHTIVA EGGFGQMTIE LVGVPLPSNP KTSTLAALSV
260
IRACRNSVEA IQI
Length:263
Mass (Da):27,954
Last modified:September 2, 2008 - v2
Checksum:iA2F94A128F512144
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000521 Genomic DNA. Translation: ABO11388.2.
RefSeqiYP_001083990.2. NC_009085.1.

Genome annotation databases

EnsemblBacteriaiABO11388; ABO11388; A1S_0956.
GeneIDi4917096.
KEGGiacb:A1S_0956.
PATRICi20718112. VBIAciBau103176_0970.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000521 Genomic DNA. Translation: ABO11388.2 .
RefSeqi YP_001083990.2. NC_009085.1.

3D structure databases

ProteinModelPortali A3M394.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 400667.A1S_0956.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO11388 ; ABO11388 ; A1S_0956 .
GeneIDi 4917096.
KEGGi acb:A1S_0956.
PATRICi 20718112. VBIAciBau103176_0970.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci ABAU400667:GI0Q-944-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. "New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
    Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
    Genes Dev. 21:601-614(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17978 / NCDC KC 755.

Entry informationi

Entry nameiASPD_ACIBT
AccessioniPrimary (citable) accession number: A3M394
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: October 1, 2014
This is version 58 of the entry and version 2 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