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Q8TS47

- ASPD_METAC

UniProt

Q8TS47 - ASPD_METAC

Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    • Comment

    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

    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.
    KOiK06989.
    OMAiECAGHSA.
    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

    MLKIGIVGCG FIGGQICRAI DGGEVSAELY ALCDSSESKA LELAASLKTC    50
    KPSYMKIEEL IRGVDLIIES ASQNAVRFIV PQALKAGCDV MILSVGALAD 100
    EELRDTLFGL AKEHNCKLYF PSGAVVGIDG LNSASAAGIS SVTLSTRKPP 150
    AGLMGAPYVV EHGIELEKLE KKTVLFEGPA SEAVKAFPAN VNVAATISLA 200
    GIGFERTRVK VIADPSLFRN VHEIIVEGEF GKFSTRVENL PSPENPKTSY 250
    LAALSAVSTL KKILNPVQIG T 271
    Length:271
    Mass (Da):28,578
    Last modified:June 1, 2002 - v1
    Checksum:i06D17290784BBBDA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010299 Genomic DNA. Translation: AAM04391.1 .
    RefSeqi NP_615911.1. NC_003552.1.

    3D structure databases

    ProteinModelPortali Q8TS47.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 188937.MA0958.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM04391 ; AAM04391 ; MA_0958 .
    GeneIDi 1472848.
    KEGGi mac:MA0958.

    Phylogenomic databases

    eggNOGi COG1712.
    KOi K06989.
    OMAi ECAGHSA.
    PhylomeDBi Q8TS47.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00456 .
    BioCyci MACE188937:GI2O-969-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 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: October 1, 2014
    This is version 77 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