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A6USM7

- ASPD_METVS

UniProt

A6USM7 - ASPD_METVS

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Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Methanococcus vannielii (strain SB / ATCC 35089 / DSM 1224)
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 sitei124 – 1241NAD; via amide nitrogenUniRule annotation
Binding sitei190 – 1901NADUniRule annotation
Active sitei218 – 2181UniRule 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

BioCyciMVAN406327:GI04-1657-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:Mevan_1607
OrganismiMethanococcus vannielii (strain SB / ATCC 35089 / DSM 1224)
Taxonomic identifieri406327 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
ProteomesiUP000001107: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Probable L-aspartate dehydrogenasePRO_1000067308Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi406327.Mevan_1607.

Structurei

3D structure databases

ProteinModelPortaliA6USM7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1712.
HOGENOMiHOG000206326.
KOiK06989.
OMAiECAGHSA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01265. NadX.
InterProiIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR022487. Asp_DH_arc.
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.
TIGRFAMsiTIGR03855. NAD_NadX. 1 hit.

Sequencei

Sequence statusi: Complete.

A6USM7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKVGIVGCG AVASLITKAL LSERIPKARV LAFYDVNYEK AKKLSEETGA
60 70 80 90 100
ESCVSIDELV SKDLDLILEC ASVSAVEETV LKSILSGKDV IIMSVGAFAN
110 120 130 140 150
KKLFLNLYKL AEEKNQKIYV PSGAVAGIDA IKAGSLGQIS DVTLTTTKPV
160 170 180 190 200
MGLKDAILDL GLKPEEITEP KVVFEGNVFE AISKFPQNIN VSVVLSLASK
210 220 230 240 250
YPAKVKIIAD PNLIVNRHEI LVKGSIGTIK TCVENNPCKD NPKTSALAAF
260
SVMRLIKDLS EPIRIGT
Length:267
Mass (Da):28,603
Last modified:August 21, 2007 - v1
Checksum:iA12E6B40833F3490
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000742 Genomic DNA. Translation: ABR55499.1.
RefSeqiYP_001324111.1. NC_009634.1.

Genome annotation databases

EnsemblBacteriaiABR55499; ABR55499; Mevan_1607.
GeneIDi5324920.
KEGGimvn:Mevan_1607.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000742 Genomic DNA. Translation: ABR55499.1 .
RefSeqi YP_001324111.1. NC_009634.1.

3D structure databases

ProteinModelPortali A6USM7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 406327.Mevan_1607.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABR55499 ; ABR55499 ; Mevan_1607 .
GeneIDi 5324920.
KEGGi mvn:Mevan_1607.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci MVAN406327:GI04-1657-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.
IPR022487. Asp_DH_arc.
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.
TIGRFAMsi TIGR03855. NAD_NadX. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SB / ATCC 35089 / DSM 1224.

Entry informationi

Entry nameiASPD_METVS
AccessioniPrimary (citable) accession number: A6USM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: October 1, 2014
This is version 50 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