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DADD_METTP
ID   DADD_METTP              Reviewed;         413 AA.
AC   A0B7V2;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=5'-deoxyadenosine deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE            Short=5'-dA deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE            EC=3.5.4.41 {ECO:0000255|HAMAP-Rule:MF_01281};
DE   AltName: Full=5'-methylthioadenosine deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE            Short=MTA deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE            EC=3.5.4.31 {ECO:0000255|HAMAP-Rule:MF_01281};
DE   AltName: Full=Adenosine deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE            EC=3.5.4.4 {ECO:0000255|HAMAP-Rule:MF_01281};
DE   AltName: Full=S-adenosylhomocysteine deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE            Short=SAH deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE            EC=3.5.4.28 {ECO:0000255|HAMAP-Rule:MF_01281};
GN   Name=dadD {ECO:0000255|HAMAP-Rule:MF_01281}; OrderedLocusNames=Mthe_0991;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the deamination of three SAM-derived enzymatic
CC       products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-
CC       methylthioadenosine, to produce the inosine analogs. Can also deaminate
CC       adenosine. The preferred substrate for this enzyme is 5'-
CC       deoxyadenosine, but all these substrates are efficiently deaminated.
CC       Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway
CC       from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent
CC       methylation reactions. May also be involved in the recycling of 5'-
CC       deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine
CC       is further metabolized to deoxyhexoses used for the biosynthesis of
CC       aromatic amino acids in methanogens. {ECO:0000255|HAMAP-Rule:MF_01281}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+);
CC         Xref=Rhea:RHEA:42892, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:28938, ChEBI:CHEBI:82775; EC=3.5.4.41;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42893;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:20716, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:57985; EC=3.5.4.28; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01281};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20717;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-
CC         thioinosine; Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:48595; EC=3.5.4.31; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01281};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25026;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC         Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01281};
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01281}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01281}.
CC   -!- MISCELLANEOUS: SAH is a product of SAM methyltransferases and is known
CC       to be a feedback inhibitor of these enzymes. As a result of this
CC       inhibition, organisms have evolved efficient enzymes to metabolize SAH
CC       via different pathways. The pathway found in methanogens differs from
CC       the canonical pathway, it uses the deamination of S-adenosyl-L-
CC       homocysteine to form S-inosyl-L-homocysteine for the regeneration of
CC       SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM
CC       enzyme reaction product which strongly inhibits radical SAM enzymes. A
CC       pathway for removing this product must be present in methanogens where
CC       the MTA/SAH nucleosidase which normally metabolizes this compound is
CC       absent. {ECO:0000255|HAMAP-Rule:MF_01281}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       MTA/SAH deaminase family. {ECO:0000255|HAMAP-Rule:MF_01281}.
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DR   EMBL; CP000477; ABK14776.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B7V2; -.
DR   SMR; A0B7V2; -.
DR   STRING; 349307.Mthe_0991; -.
DR   EnsemblBacteria; ABK14776; ABK14776; Mthe_0991.
DR   KEGG; mtp:Mthe_0991; -.
DR   HOGENOM; CLU_012358_2_1_2; -.
DR   OMA; ALIGKVC; -.
DR   UniPathway; UPA00315; -.
DR   Proteomes; UP000000674; Chromosome.
DR   GO; GO:0090613; F:5'-deoxyadenosine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0090614; F:5'-methylthioadenosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050270; F:S-adenosylhomocysteine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_01281; MTA_SAH_deamin; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR023512; Deaminase_MtaD/DadD.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..413
FT                   /note="5'-deoxyadenosine deaminase"
FT                   /id="PRO_0000312478"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ   SEQUENCE   413 AA;  46382 MW;  FE23B69FDED9B8DC CRC64;
     MLIRSASIIR NGSLLKNIDI LIEGNRISEV GRDLRPNDDE IIDARNMLAV PGLVNSHTHL
     AMTLLRGYAD DMELIPWLQE KIWPLEARLK PSDVRAGVKL GCLELIRFGV TCYNDMYYFM
     DETAAATREM GIRGVLSGVL FDMRPEFIND VEPFIKKWRD DDLIKPAVGP HAVYTCSEET
     LLRAKDIAER YDVKIHIHLS ETRDEVDTFV NQRHMSPVEY LENLGFLSER VVAAHCVWLT
     PRDIRILAER HVNVAHCPIS NLKLASGIAP VATLIEHGVN VCLGTDGASS NNNLDIFEEM
     KVAAVVQKCS VGRSAILPAD AVWRMATENA YKAFSLDMGI RRGALADLAL INMRRPWFIP
     VTSMISHLVY SMSGEASYTI CNGRVLMRDG VIEGEAKILD EAQRCYERLI SEE
 
 
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