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A9SS00

- MTND2_PHYPA

UniProt

A9SS00 - MTND2_PHYPA

Protein

1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 2

Gene

PHYPADRAFT_134384

Organism
Physcomitrella patens subsp. patens (Moss)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).UniRule annotation

    Catalytic activityi

    1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 4-(methylthio)-2-oxobutanoate + formate.UniRule annotation

    Cofactori

    Binds 1 iron ion per monomer. Can also use other divalent metal cations.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi94 – 941Iron or nickelUniRule annotation
    Metal bindingi96 – 961Iron or nickelUniRule annotation
    Metal bindingi100 – 1001Iron or nickelUniRule annotation
    Metal bindingi139 – 1391Iron or nickelUniRule annotation

    GO - Molecular functioni

    1. acireductone dioxygenase [iron(II)-requiring] activity Source: UniProtKB-HAMAP
    2. iron ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. L-methionine biosynthetic process from methylthioadenosine Source: UniProtKB-HAMAP
    2. regulation of cell division Source: EnsemblPlants/Gramene

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00904; UER00878.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 2UniRule annotation (EC:1.13.11.54UniRule annotation)
    Alternative name(s):
    Acireductone dioxygenase (Fe(2+)-requiring) 2UniRule annotation
    Short name:
    ARD 2UniRule annotation
    Short name:
    Fe-ARD 2UniRule annotation
    Gene namesi
    ORF Names:PHYPADRAFT_134384
    OrganismiPhyscomitrella patens subsp. patens (Moss)
    Taxonomic identifieri3218 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaBryophytaBryophytinaBryopsidaFunariidaeFunarialesFunariaceaePhyscomitrella
    ProteomesiUP000006727: Partially assembled WGS sequence

    Subcellular locationi

    Cytoplasm UniRule annotation. Nucleus UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1951951,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 2PRO_0000414343Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi3218.JGI134384.

    Structurei

    3D structure databases

    ProteinModelPortaliA9SS00.
    SMRiA9SS00. Positions 8-178.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acireductone dioxygenase (ARD) family.UniRule annotation

    Phylogenomic databases

    KOiK08967.

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    HAMAPiMF_03154. Salvage_MtnD_euk.
    InterProiIPR004313. Acireductn_dOase_family.
    IPR027496. MTCBP-1_eukaryotes.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PANTHERiPTHR23418. PTHR23418. 1 hit.
    PfamiPF03079. ARD. 1 hit.
    [Graphical view]
    SUPFAMiSSF51182. SSF51182. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A9SS00-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQVQRPPLEA WYMNDSEEDQ RLPHHRNPPE YVTLEKLAAL GVIHWVLDAD    50
    NHETDPELSI IRKDRGYNYT DVITVCPEML PSYEAKIKSF YEEHIHMDEE 100
    IRYCLDGSGY FDVRDPEDHW IRIWVRKGDM IVLPAGCYHR FTLDEHNYIM 150
    AMRLFVGEPI WTPYNRPQDE HPVRKGYVHQ FLQPELLDVD MSISA 195
    Length:195
    Mass (Da):23,199
    Last modified:February 5, 2008 - v1
    Checksum:iD0AED4C8E9A82C70
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS545000 Genomic DNA. Translation: EDQ66042.1.
    RefSeqiXP_001769170.1. XM_001769118.1.

    Genome annotation databases

    GeneIDi5932378.
    KEGGippp:PHYPADRAFT_134384.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS545000 Genomic DNA. Translation: EDQ66042.1 .
    RefSeqi XP_001769170.1. XM_001769118.1.

    3D structure databases

    ProteinModelPortali A9SS00.
    SMRi A9SS00. Positions 8-178.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3218.JGI134384.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5932378.
    KEGGi ppp:PHYPADRAFT_134384.

    Phylogenomic databases

    KOi K08967.

    Enzyme and pathway databases

    UniPathwayi UPA00904 ; UER00878 .

    Family and domain databases

    Gene3Di 2.60.120.10. 1 hit.
    HAMAPi MF_03154. Salvage_MtnD_euk.
    InterProi IPR004313. Acireductn_dOase_family.
    IPR027496. MTCBP-1_eukaryotes.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view ]
    PANTHERi PTHR23418. PTHR23418. 1 hit.
    Pfami PF03079. ARD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51182. SSF51182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The Physcomitrella genome reveals evolutionary insights into the conquest of land by plants."
      Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., Suzuki Y.
      , Hashimoto S.-I., Yamaguchi K., Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., Boore J.L.
      Science 319:64-69(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Gransden 2004.

    Entry informationi

    Entry nameiMTND2_PHYPA
    AccessioniPrimary (citable) accession number: A9SS00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 14, 2011
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 39 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    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