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Q8PV99

- ASPD_METMA

UniProt

Q8PV99 - ASPD_METMA

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Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
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 sitei192 – 1921NADUniRule annotation
Active sitei222 – 2221UniRule 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

BioCyciMMAZ192952:GCK2-2126-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:MM_2072
OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Taxonomic identifieri192952 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000000595: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Probable L-aspartate dehydrogenasePRO_0000144898Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi192952.MM_2072.

Structurei

3D structure databases

ProteinModelPortaliQ8PV99.
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.

Q8PV99-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKIGIIGCG FIGGQICRAI DSGEIDAELY ALCDSSESKA FGLAKSLNTC
60 70 80 90 100
KPAYMKIEEL ISSVDLVVES ASQNAVRFIV PQALKAGCSV MVLSVGALAD
110 120 130 140 150
KELRETLFGL AKKHNCKLYF PSGAVVGIDG INSAHAAGIS SVTLTTRKPP
160 170 180 190 200
SGLMGAPYVV EHGIELEKLE KETILFEGTA SEAVKAFPAN VNVAATISLA
210 220 230 240 250
GIGFERTMVR VIADPSLSRN IHEINVEGEF GKFCTKVENL PSPENPKTSY
260 270
LAALSAISTL KKILNPVQIG T
Length:271
Mass (Da):28,615
Last modified:August 16, 2005 - v2
Checksum:i466E329688C58EC3
GO

Sequence cautioni

The sequence AAM31768.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008384 Genomic DNA. Translation: AAM31768.1. Different initiation.
RefSeqiNP_634096.1. NC_003901.1.

Genome annotation databases

EnsemblBacteriaiAAM31768; AAM31768; MM_2072.
GeneIDi1480414.
KEGGimma:MM_2072.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008384 Genomic DNA. Translation: AAM31768.1 . Different initiation.
RefSeqi NP_634096.1. NC_003901.1.

3D structure databases

ProteinModelPortali Q8PV99.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 192952.MM_2072.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM31768 ; AAM31768 ; MM_2072 .
GeneIDi 1480414.
KEGGi mma:MM_2072.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci MMAZ192952:GCK2-2126-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. "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
    Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R.
    , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
    J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Entry informationi

Entry nameiASPD_METMA
AccessioniPrimary (citable) accession number: Q8PV99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: October 1, 2014
This is version 77 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, 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