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Q6LZ92

- ASPD_METMP

UniProt

Q6LZ92 - ASPD_METMP

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Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Methanococcus maripaludis (strain S2 / LL)
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

BioCyciMMAR267377:GJ77-766-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:MMP0737
OrganismiMethanococcus maripaludis (strain S2 / LL)
Taxonomic identifieri267377 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
ProteomesiUP000000590: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Probable L-aspartate dehydrogenasePRO_0000144899Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi267377.MMP0737.

Structurei

3D structure databases

ProteinModelPortaliQ6LZ92.
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.

Q6LZ92-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKIGLVGCG AIASLITKAL MSDRLNKAEV LAFYDGNLEK AEKLAMETGA
60 70 80 90 100
DFCKSLDELV SKDLDLIVEC ASVNAVEDTV IKSLNNDKDV IIMSVGAFAD
110 120 130 140 150
KDLFVKLYKL AEKLGKKIYV PSGAVAGIDA VKSGSLGKIS EVSLTTTKPV
160 170 180 190 200
HGLKSALEEQ GLNTDEIKEP KIVFEGTVFD AISKFPQNIN VSVVLSLASR
210 220 230 240 250
YPAKVKIIAD PNAVVNRHEI LVKGSIGTIK TCVENNPCRD NPKTSALAAY
260
SVIRLIKDLS EPVRIGT
Length:267
Mass (Da):28,593
Last modified:July 5, 2004 - v1
Checksum:i061F6D2566E0E33A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX950229 Genomic DNA. Translation: CAF30293.1.
RefSeqiNP_987857.1. NC_005791.1.

Genome annotation databases

EnsemblBacteriaiCAF30293; CAF30293; MMP0737.
GeneIDi2761445.
KEGGimmp:MMP0737.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX950229 Genomic DNA. Translation: CAF30293.1 .
RefSeqi NP_987857.1. NC_005791.1.

3D structure databases

ProteinModelPortali Q6LZ92.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 267377.MMP0737.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAF30293 ; CAF30293 ; MMP0737 .
GeneIDi 2761445.
KEGGi mmp:MMP0737.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci MMAR267377:GJ77-766-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: S2 / LL.

Entry informationi

Entry nameiASPD_METMP
AccessioniPrimary (citable) accession number: Q6LZ92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 5, 2004
Last modified: October 1, 2014
This is version 68 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3