ID A0A0E3QWJ6_METBA Unreviewed; 432 AA. AC A0A0E3QWJ6; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 05-JUN-2019, entry version 20. 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 CC 5'-methylthioadenosine, to produce the inosine analogs. Can also CC deaminate adenosine. The preferred substrate for this enzyme is CC 5'-deoxyadenosine, but all these substrates are efficiently CC deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) CC recycling pathway from S-adenosyl-L-homocysteine (SAH) produced CC from SAM-dependent methylation reactions. May also be involved in CC the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose CC moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses CC used for the biosynthesis of aromatic amino acids in methanogens. CC {ECO:0000256|HAMAP-Rule:MF_01281}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + CC NH4(+); Xref=Rhea:RHEA:42892, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:82775; EC=3.5.4.41; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01281}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S- CC inosyl-L-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- CC methyl-5'-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; CC EC=3.5.4.4; Evidence={ECO:0000256|HAMAP-Rule:MF_01281}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01281}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01281}; CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine CC biosynthesis. {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 CC known to be a feedback inhibitor of these enzymes. As a result of CC this inhibition, organisms have evolved efficient enzymes to CC metabolize SAH via different pathways. The pathway found in CC methanogens differs from the canonical pathway, it uses the CC deamination of S-adenosyl-L-homocysteine to form S-inosyl-L- CC homocysteine for the regeneration of SAM from S-adenosyl-L- CC homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction CC product which strongly inhibits radical SAM enzymes. A pathway for CC removing this product must be present in methanogens where the CC 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 CC superfamily. MTA/SAH deaminase family. {ECO:0000256|HAMAP- CC Rule:MF_01281}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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 KO; K12960; -. DR UniPathway; UPA00315; -. DR Proteomes; UP000033033; Chromosome. DR GO; GO:0090613; F:5'-deoxyadenosine deaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 Complete proteome {ECO:0000313|Proteomes:UP000033033}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01281, KW 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 Amidohydro-rel. {ECO:0000259|Pfam: FT PF01979}. FT METAL 63 63 Zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01281}. FT METAL 65 65 Zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01281}. FT METAL 211 211 Zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01281}. FT METAL 299 299 Zinc. {ECO:0000256|HAMAP-Rule:MF_01281}. FT BINDING 92 92 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01281}. FT BINDING 184 184 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01281}. FT BINDING 214 214 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01281}. FT BINDING 299 299 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //