Skip Header

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

Q62BI3

- ASPD_BURMA

UniProt

Q62BI3 - ASPD_BURMA

(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 mallei (strain ATCC 23344)
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

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:BMAA1329
OrganismiBurkholderia mallei (strain ATCC 23344)
Taxonomic identifieri243160 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000006693: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Probable L-aspartate dehydrogenasePRO_0000144888Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243160.BMAA1329.

Structurei

3D structure databases

ProteinModelPortaliQ62BI3.
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.

Q62BI3-1 [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:October 25, 2004 - v1
Checksum:i5703F6D14871D311
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000011 Genomic DNA. Translation: AAU46671.1.
RefSeqiYP_105945.1. NC_006349.2.

Genome annotation databases

EnsemblBacteriaiAAU46671; AAU46671; BMAA1329.
GeneIDi3087458.
KEGGibma:BMAA1329.
PATRICi19124813. VBIBurMal55007_4889.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000011 Genomic DNA. Translation: AAU46671.1 .
RefSeqi YP_105945.1. NC_006349.2.

3D structure databases

ProteinModelPortali Q62BI3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243160.BMAA1329.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU46671 ; AAU46671 ; BMAA1329 .
GeneIDi 3087458.
KEGGi bma:BMAA1329.
PATRICi 19124813. VBIBurMal55007_4889.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .

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: ATCC 23344.

Entry informationi

Entry nameiASPD_BURMA
AccessioniPrimary (citable) accession number: Q62BI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 25, 2004
Last modified: October 1, 2014
This is version 70 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