DADD_METAC
ID DADD_METAC Reviewed; 432 AA.
AC Q8TRA4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=MA_1276;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM04695.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE010299; AAM04695.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048065074.1; NC_003552.1.
DR AlphaFoldDB; Q8TRA4; -.
DR SMR; Q8TRA4; -.
DR STRING; 188937.MA_1276; -.
DR EnsemblBacteria; AAM04695; AAM04695; MA_1276.
DR GeneID; 1473164; -.
DR KEGG; mac:MA_1276; -.
DR HOGENOM; CLU_012358_2_1_2; -.
DR InParanoid; Q8TRA4; -.
DR OMA; ALIGKVC; -.
DR OrthoDB; 40873at2157; -.
DR PhylomeDB; Q8TRA4; -.
DR UniPathway; UPA00315; -.
DR Proteomes; UP000002487; 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..432
FT /note="5'-deoxyadenosine deaminase"
FT /id="PRO_0000312479"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ SEQUENCE 432 AA; 47157 MW; 8FAAAF51C4DF4441 CRC64;
MADIIIKNAY VLTMDPDAGD LKNGTVVIED GKITEIGENT KENADTVIDA KGSVVMPGLA
NTHTHAAMTL FRGYADDLQL AEWLEKHIWP AEAQLKAEDV YKGSLLACLE MIKSGTTSFA
DMYFYMDETA KAVEASGLRA SLSHGLIELW NEEKGEADLK EGKRFVRAWQ GAADGRIKTM
YGPHAPNTCS EEFLTKVKEE AHRDGAGLHI HVLETEAELN AMKERYGKCS VHLLEDIGFF
GPDVLAAHCV WLSDGDIEIL RQREVNVSHN PISNMKLASG IAPVYKMLEK GVNVTLGTDG
CASNNNLDLF EEIKTAALLH KVSTGNPTAL PARQVLEMAT VNGAKALGTE TGMLKVGKKA
DMIVVDMKKP HLTPCFDVPS HLVYSAKGCD VRTTIVDGKV LMDNYRVLVM DEEKVIEEAR
TAAEELVARA NA
