ID A0A0E3QWJ6_METBA Unreviewed; 432 AA. AC A0A0E3QWJ6; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 26-FEB-2020, entry version 23. DE RecName: Full=5'-deoxyadenosine deaminase {ECO:0000256|HAMAP-Rule:MF_01281}; DE Short=5'-dA deaminase {ECO:0000256|HAMAP-Rule:MF_01281}; DE EC=3.5.4.41 {ECO:0000256|HAMAP-Rule:MF_01281}; DE AltName: Full=5'-methylthioadenosine deaminase {ECO:0000256|HAMAP-Rule:MF_01281}; DE Short=MTA deaminase {ECO:0000256|HAMAP-Rule:MF_01281}; DE EC=3.5.4.31 {ECO:0000256|HAMAP-Rule:MF_01281}; DE AltName: Full=Adenosine deaminase {ECO:0000256|HAMAP-Rule:MF_01281}; DE EC=3.5.4.4 {ECO:0000256|HAMAP-Rule:MF_01281}; DE AltName: Full=S-adenosylhomocysteine deaminase {ECO:0000256|HAMAP-Rule:MF_01281}; DE Short=SAH deaminase {ECO:0000256|HAMAP-Rule:MF_01281}; DE EC=3.5.4.28 {ECO:0000256|HAMAP-Rule:MF_01281}; GN Name=dadD {ECO:0000256|HAMAP-Rule:MF_01281}; GN ORFNames=MSBRM_2087 {ECO:0000313|EMBL:AKB55085.1}; OS Methanosarcina barkeri MS. OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=1434108 {ECO:0000313|EMBL:AKB55085.1, ECO:0000313|Proteomes:UP000033033}; RN [1] {ECO:0000313|EMBL:AKB55085.1, ECO:0000313|Proteomes:UP000033033} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MS {ECO:0000313|EMBL:AKB55085.1, RC ECO:0000313|Proteomes:UP000033033}; RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D., RA Metcalf M.E., Whitaker R.J., Metcalf W.W.; RT "Methanogenic archaea and the global carbon cycle."; RL Submitted (JUL-2014) 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:0000256|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:0000256|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:0000256|HAMAP- CC 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:0000256|HAMAP- CC 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:0000256|HAMAP-Rule:MF_01281}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01281}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01281}; CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_01281}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01281}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC MTA/SAH deaminase family. {ECO:0000256|HAMAP-Rule:MF_01281}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01281}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP009528; AKB55085.1; -; Genomic_DNA. DR RefSeq; WP_048116906.1; NZ_CP009528.1. DR EnsemblBacteria; AKB55085; AKB55085; MSBRM_2087. DR GeneID; 24884007; -. DR KEGG; mby:MSBRM_2087; -. DR PATRIC; fig|1434108.4.peg.2659; -. DR HOGENOM; CLU_012358_2_1_2; -. DR KO; K12960; -. DR UniPathway; UPA00315; -. DR Proteomes; UP000033033; Chromosome. DR GO; GO:0090613; F:5'-deoxyadenosine deaminase activity; IEA:UniProtKB-UniRule. 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 {ECO:0000256|HAMAP-Rule:MF_01281, ECO:0000313|EMBL:AKB55085.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01281}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01281}. FT DOMAIN 54..400 FT /note="Amidohydro-rel" FT /evidence="ECO:0000259|Pfam:PF01979" FT METAL 63 FT /note="Zinc; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281" FT METAL 65 FT /note="Zinc; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281" FT METAL 211 FT /note="Zinc; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281" FT METAL 299 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281" FT BINDING 92 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281" FT BINDING 184 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281" FT BINDING 214 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281" FT BINDING 299 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281" SQ SEQUENCE 432 AA; 46937 MW; 3359D4929A8022BB CRC64; MADIIVKNAY VLTMDPDAGD LKNGTVVIED GKITEIGEKT SESADTVIDA KHSVVMPGLV NTHTHAAMTL FRGYADDLQL ADWLEGHIWP AEAKLTADDV YKGSLLACLE MIRSGTTSFA DMYFYMDETA KAVEASGLRA SLCHGLIELW NEEKGATDLK EGKRFVRAWQ GAADGRIKTM YGPHAPNTCS EEYLAKVREE ANRDGAGIHI HLLETEAELL AMKERYGKCS VHLLEDIGFL GPDVLAAHCV WLSDGDIEIL GKRGVNVSHN VISNMKLASG IAPVHKMLEK GVNVSLGTDG CASNNNLDLF EEMKTAALLH KVNTFSPTAL PARQVLQMGT VNGAKALGTE TGMLKVGMKA DLIVVDMKKP HLTPCFNVPS HLVYSAKGSD VRTTIVNGKV LMDDYKVLVL DEQKVMEETQ KAAEELVARV NA //