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Protein

5-methylthioadenosine/S-adenosylhomocysteine deaminase

Gene

mtaD

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine. Adenosine-5-monophosphate (AMP) and S-adenosyl-L-methionine (SAM) are not enzyme substrates.1 Publication

Catalytic activityi

S-adenosyl-L-homocysteine + H2O = S-inosyl-L-homocysteine + NH3.1 Publication
S-methyl-5'-thioadenosine + H2O = S-methyl-5'-thioinosine + NH3.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Kineticsi

  1. KM=210 µM for S-adenosyl-L-homocysteine1 Publication
  2. KM=44 µM for 5-methyl-thioadenosine1 Publication
  3. KM=250 µM for adenosine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi55 – 551Zinc; via tele nitrogen
    Metal bindingi57 – 571Zinc; via tele nitrogen
    Binding sitei84 – 841Substrate
    Binding sitei136 – 1361Substrate
    Binding sitei148 – 1481Substrate
    Binding sitei173 – 1731Substrate
    Metal bindingi200 – 2001Zinc; via tele nitrogen
    Binding sitei203 – 2031Substrate
    Metal bindingi279 – 2791Zinc
    Binding sitei279 – 2791Substrate

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16147.
    BRENDAi3.5.4.31. 6331.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5-methylthioadenosine/S-adenosylhomocysteine deaminase (EC:3.5.4.28, EC:3.5.4.31)
    Short name:
    MTA/SAH deaminase
    Gene namesi
    Name:mtaD
    Ordered Locus Names:TM_0936
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    Proteomesi
    • UP000008183 Componenti: Chromosome

    Pathology & Biotechi

    Chemistry

    ChEMBLiCHEMBL1075031.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4064065-methylthioadenosine/S-adenosylhomocysteine deaminasePRO_0000312465Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi243274.TM0936.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 87Combined sources
    Beta strandi17 – 248Combined sources
    Beta strandi27 – 359Combined sources
    Beta strandi39 – 413Combined sources
    Beta strandi45 – 495Combined sources
    Beta strandi51 – 566Combined sources
    Helixi58 – 636Combined sources
    Helixi72 – 776Combined sources
    Helixi80 – 845Combined sources
    Helixi89 – 10416Combined sources
    Turni105 – 1073Combined sources
    Beta strandi108 – 11710Combined sources
    Helixi118 – 12811Combined sources
    Beta strandi131 – 1388Combined sources
    Helixi148 – 15912Combined sources
    Helixi162 – 1643Combined sources
    Beta strandi166 – 1727Combined sources
    Turni175 – 1773Combined sources
    Helixi180 – 19213Combined sources
    Beta strandi197 – 2026Combined sources
    Helixi212 – 2154Combined sources
    Turni216 – 2216Combined sources
    Beta strandi224 – 2285Combined sources
    Helixi234 – 2363Combined sources
    Turni237 – 2426Combined sources
    Beta strandi243 – 2497Combined sources
    Helixi251 – 2566Combined sources
    Helixi264 – 2696Combined sources
    Beta strandi273 – 2764Combined sources
    Turni281 – 2844Combined sources
    Helixi289 – 30113Combined sources
    Helixi310 – 3178Combined sources
    Helixi319 – 3257Combined sources
    Beta strandi340 – 3445Combined sources
    Helixi348 – 3503Combined sources
    Helixi353 – 3553Combined sources
    Helixi356 – 3627Combined sources
    Beta strandi369 – 3735Combined sources
    Beta strandi376 – 3805Combined sources
    Helixi389 – 40315Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J6PX-ray1.90A1-406[»]
    1P1MX-ray1.50A1-406[»]
    2PLMX-ray2.10A1-406[»]
    ProteinModelPortaliQ9X034.
    SMRiQ9X034. Positions 1-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X034.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MTA/SAH deaminase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105D6T. Bacteria.
    COG0402. LUCA.
    InParanoidiQ9X034.
    KOiK12960.
    OMAiCSEETYQ.
    OrthoDBiEOG65QWFB.

    Family and domain databases

    Gene3Di2.30.40.10. 2 hits.
    HAMAPiMF_01281. MTA_SAH_deamin.
    InterProiIPR006680. Amidohydro-rel.
    IPR023512. Deaminase_MtaD/DadD.
    IPR011059. Metal-dep_hydrolase_composite.
    IPR032466. Metal_Hydrolase.
    [Graphical view]
    PfamiPF01979. Amidohydro_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF51338. SSF51338. 2 hits.
    SSF51556. SSF51556. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9X034-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIIGNCLILK DFSSEPFWGA VEIENGTIKR VLQGEVKVDL DLSGKLVMPA
    60 70 80 90 100
    LFNTHTHAPM TLLRGVAEDL SFEEWLFSKV LPIEDRLTEK MAYYGTILAQ
    110 120 130 140 150
    MEMARHGIAG FVDMYFHEEW IAKAVRDFGM RALLTRGLVD SNGDDGGRLE
    160 170 180 190 200
    ENLKLYNEWN GFEGRIFVGF GPHSPYLCSE EYLKRVFDTA KSLNAPVTIH
    210 220 230 240 250
    LYETSKEEYD LEDILNIGLK EVKTIAAHCV HLPERYFGVL KDIPFFVSHN
    260 270 280 290 300
    PASNLKLGNG IAPVQRMIEH GMKVTLGTDG AASNNSLNLF FEMRLASLLQ
    310 320 330 340 350
    KAQNPRNLDV NTCLKMVTYD GAQAMGFKSG KIEEGWNADL VVIDLDLPEM
    360 370 380 390 400
    FPVQNIKNHL VHAFSGEVFA TMVAGKWIYF DGEYPTIDSE EVKRELARIE

    KELYSS
    Length:406
    Mass (Da):45,773
    Last modified:November 1, 1999 - v1
    Checksum:i3437565703ECC544
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36017.1.
    PIRiH72315.
    RefSeqiNP_228744.1. NC_000853.1.
    WP_004080626.1. NZ_CP011107.1.

    Genome annotation databases

    EnsemblBacteriaiAAD36017; AAD36017; TM_0936.
    GeneIDi898610.
    KEGGitma:TM0936.
    PATRICi23936803. VBITheMar51294_0950.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36017.1.
    PIRiH72315.
    RefSeqiNP_228744.1. NC_000853.1.
    WP_004080626.1. NZ_CP011107.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J6PX-ray1.90A1-406[»]
    1P1MX-ray1.50A1-406[»]
    2PLMX-ray2.10A1-406[»]
    ProteinModelPortaliQ9X034.
    SMRiQ9X034. Positions 1-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243274.TM0936.

    Chemistry

    ChEMBLiCHEMBL1075031.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD36017; AAD36017; TM_0936.
    GeneIDi898610.
    KEGGitma:TM0936.
    PATRICi23936803. VBITheMar51294_0950.

    Phylogenomic databases

    eggNOGiENOG4105D6T. Bacteria.
    COG0402. LUCA.
    InParanoidiQ9X034.
    KOiK12960.
    OMAiCSEETYQ.
    OrthoDBiEOG65QWFB.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16147.
    BRENDAi3.5.4.31. 6331.

    Miscellaneous databases

    EvolutionaryTraceiQ9X034.

    Family and domain databases

    Gene3Di2.30.40.10. 2 hits.
    HAMAPiMF_01281. MTA_SAH_deamin.
    InterProiIPR006680. Amidohydro-rel.
    IPR023512. Deaminase_MtaD/DadD.
    IPR011059. Metal-dep_hydrolase_composite.
    IPR032466. Metal_Hydrolase.
    [Graphical view]
    PfamiPF01979. Amidohydro_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF51338. SSF51338. 2 hits.
    SSF51556. SSF51556. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. "Structure-based activity prediction for an enzyme of unknown function."
      Hermann J.C., Marti-Arbona R., Fedorov A.A., Fedorov E., Almo S.C., Shoichet B.K., Raushel F.M.
      Nature 448:775-779(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-5, X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ZINC ION AND PRODUCT, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM.
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    3. "Structure of the hypothetical protein TM0936 from Thermotoga maritima at 1.5 A bound to Ni and methionine."
      New York structural genomics research consortium (NYSGRC)
      Submitted (JAN-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH NICKEL ION AND METHIONINE.
    4. "Crystal structure of metal-dependent hydrolase of cytosinedemaniase/chlorohydrolase family (TM0936) from Thermotoga maritima at 1.9 A resolution."
      Joint center for structural genomics (JCSG)
      Submitted (MAR-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NICKEL ION.

    Entry informationi

    Entry nameiMTAD_THEMA
    AccessioniPrimary (citable) accession number: Q9X034
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 4, 2007
    Last sequence update: November 1, 1999
    Last modified: April 13, 2016
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    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 one 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.