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Q58325

- ASPD_METJA

UniProt

Q58325 - ASPD_METJA

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Protein

Probable L-aspartate dehydrogenase

Gene
nadX, MJ0915
Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
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 By similarity.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 nitrogen By similarity
Binding sitei190 – 1901NAD By similarity
Active sitei218 – 2181 By similarity

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 dehydrogenase (EC:1.4.1.21)
Gene namesi
Name:nadX
Ordered Locus Names:MJ0915
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
ProteomesiUP000000805: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Probable L-aspartate dehydrogenaseUniRule annotationPRO_0000144896Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243232.MJ0915.

Structurei

3D structure databases

ProteinModelPortaliQ58325.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1712.
KOiK06989.
OMAiECAGHSA.
PhylomeDBiQ58325.

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.

Q58325-1 [UniParc]FASTAAdd to Basket

« Hide

MLKIGIVGCG AIGNFITKKV LDGTIKNAKI SAVYDRNFDK AKTLSERTGA    50
KICSSIDDLV KEDLDLVVEA ASIKAVEEIA EKSLINNKDV LIMSVGALAD 100
KKLFLKLRDL AKTVGRKIYL PSGAIGGLDA IKALRLGEIE EVVLKTTKPV 150
AALEDALKNL GYKPEDIKNP VIVFEGDVFK AIKEFPANIN VSVTLSIAAE 200
FPAKVVIVAD PNAKLNKHEL FVKSSIGTLR VCIENVPFEE NPRTSALAAY 250
SAVRLIRDLA EPVKVGT 267
Length:267
Mass (Da):28,755
Last modified:November 1, 1996 - v1
Checksum:iB2C427DFD3AE1A4F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB98920.1.
PIRiC64414.
RefSeqiNP_247910.1. NC_000909.1.
WP_010870429.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB98920; AAB98920; MJ_0915.
GeneIDi1451804.
KEGGimja:MJ_0915.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB98920.1 .
PIRi C64414.
RefSeqi NP_247910.1. NC_000909.1.
WP_010870429.1. NC_000909.1.

3D structure databases

ProteinModelPortali Q58325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243232.MJ0915.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB98920 ; AAB98920 ; MJ_0915 .
GeneIDi 1451804.
KEGGi mja:MJ_0915.

Phylogenomic databases

eggNOGi COG1712.
KOi K06989.
OMAi ECAGHSA.
PhylomeDBi Q58325.

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.
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: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Entry informationi

Entry nameiASPD_METJA
AccessioniPrimary (citable) accession number: Q58325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 90 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 By similarity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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