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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)DescriptionActionsGraphical viewLength
    Metal bindingi55Zinc; via tele nitrogen1
    Metal bindingi57Zinc; via tele nitrogen1
    Binding sitei84Substrate1
    Binding sitei136Substrate1
    Binding sitei148Substrate1
    Binding sitei173Substrate1
    Metal bindingi200Zinc; via tele nitrogen1
    Binding sitei203Substrate1
    Metal bindingi279Zinc1
    Binding sitei279Substrate1

    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 databases

    ChEMBLiCHEMBL1075031.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003124651 – 4065-methylthioadenosine/S-adenosylhomocysteine deaminaseAdd BLAST406

    Interactioni

    Protein-protein interaction databases

    STRINGi243274.TM0936.

    Structurei

    Secondary structure

    1406
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 8Combined sources7
    Beta strandi17 – 24Combined sources8
    Beta strandi27 – 35Combined sources9
    Beta strandi39 – 41Combined sources3
    Beta strandi45 – 49Combined sources5
    Beta strandi51 – 56Combined sources6
    Helixi58 – 63Combined sources6
    Helixi72 – 77Combined sources6
    Helixi80 – 84Combined sources5
    Helixi89 – 104Combined sources16
    Turni105 – 107Combined sources3
    Beta strandi108 – 117Combined sources10
    Helixi118 – 128Combined sources11
    Beta strandi131 – 138Combined sources8
    Helixi148 – 159Combined sources12
    Helixi162 – 164Combined sources3
    Beta strandi166 – 172Combined sources7
    Turni175 – 177Combined sources3
    Helixi180 – 192Combined sources13
    Beta strandi197 – 202Combined sources6
    Helixi212 – 215Combined sources4
    Turni216 – 221Combined sources6
    Beta strandi224 – 228Combined sources5
    Helixi234 – 236Combined sources3
    Turni237 – 242Combined sources6
    Beta strandi243 – 249Combined sources7
    Helixi251 – 256Combined sources6
    Helixi264 – 269Combined sources6
    Beta strandi273 – 276Combined sources4
    Turni281 – 284Combined sources4
    Helixi289 – 301Combined sources13
    Helixi310 – 317Combined sources8
    Helixi319 – 325Combined sources7
    Beta strandi340 – 344Combined sources5
    Helixi348 – 350Combined sources3
    Helixi353 – 355Combined sources3
    Helixi356 – 362Combined sources7
    Beta strandi369 – 373Combined sources5
    Beta strandi376 – 380Combined sources5
    Helixi389 – 403Combined sources15

    3D structure databases

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

    Family and domain databases

    Gene3Di2.30.40.10. 2 hits.
    HAMAPiMF_01281. MTA_SAH_deamin. 1 hit.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1J6PX-ray1.90A1-406[»]
    1P1MX-ray1.50A1-406[»]
    2PLMX-ray2.10A1-406[»]
    ProteinModelPortaliQ9X034.
    SMRiQ9X034.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243274.TM0936.

    Chemistry databases

    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.
    OMAiVPFHTHI.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ9X034.
    PROiQ9X034.

    Family and domain databases

    Gene3Di2.30.40.10. 2 hits.
    HAMAPiMF_01281. MTA_SAH_deamin. 1 hit.
    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...

    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: November 2, 2016
    This is version 104 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.