ID A0A0E3QWJ6_METBA Unreviewed; 432 AA. AC A0A0E3QWJ6; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 16-JAN-2019, entry version 19. 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}; 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 5'-deoxyadenosine into 5'- CC deoxyinosine. May be involved in the recycling of 5'- CC deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'- CC deoxyinosine is further metabolized to deoxyhexoses used for the CC biosynthesis of aromatic amino acids in methanogens. Is also able CC to deaminate 5-methylthioadenosine, S-adenosyl-L-homocysteine and CC adenosine to a small extent. {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 -!- 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 -!- 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 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 //