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Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Status
Reviewed-Annotation score: 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

BioCyciMACE188937:GI2O-969-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:MA_0958
OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifieri188937 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000002487: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Probable L-aspartate dehydrogenasePRO_0000144895Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi188937.MA0958.

Structurei

3D structure databases

ProteinModelPortaliQ8TS47.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1712.
InParanoidiQ8TS47.
KOiK06989.
OMAiPKTSYLA.
PhylomeDBiQ8TS47.

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.

Q8TS47-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKIGIVGCG FIGGQICRAI DGGEVSAELY ALCDSSESKA LELAASLKTC
60 70 80 90 100
KPSYMKIEEL IRGVDLIIES ASQNAVRFIV PQALKAGCDV MILSVGALAD
110 120 130 140 150
EELRDTLFGL AKEHNCKLYF PSGAVVGIDG LNSASAAGIS SVTLSTRKPP
160 170 180 190 200
AGLMGAPYVV EHGIELEKLE KKTVLFEGPA SEAVKAFPAN VNVAATISLA
210 220 230 240 250
GIGFERTRVK VIADPSLFRN VHEIIVEGEF GKFSTRVENL PSPENPKTSY
260 270
LAALSAVSTL KKILNPVQIG T
Length:271
Mass (Da):28,578
Last modified:June 1, 2002 - v1
Checksum:i06D17290784BBBDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM04391.1.
RefSeqiNP_615911.1. NC_003552.1.

Genome annotation databases

EnsemblBacteriaiAAM04391; AAM04391; MA_0958.
GeneIDi1472848.
KEGGimac:MA0958.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM04391.1.
RefSeqiNP_615911.1. NC_003552.1.

3D structure databases

ProteinModelPortaliQ8TS47.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi188937.MA0958.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM04391; AAM04391; MA_0958.
GeneIDi1472848.
KEGGimac:MA0958.

Phylogenomic databases

eggNOGiCOG1712.
InParanoidiQ8TS47.
KOiK06989.
OMAiPKTSYLA.
PhylomeDBiQ8TS47.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00456.
BioCyciMACE188937:GI2O-969-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. "The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
    Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.
    , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.
    Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

Entry informationi

Entry nameiASPD_METAC
AccessioniPrimary (citable) accession number: Q8TS47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2002
Last modified: February 4, 2015
This is version 81 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.