ID A0A0E3S1S1_9EURY Unreviewed; 432 AA.
AC A0A0E3S1S1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=MSLAZ_0770 {ECO:0000313|EMBL:AKB74031.1};
OS Methanosarcina lacustris Z-7289.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434111 {ECO:0000313|EMBL:AKB74031.1, ECO:0000313|Proteomes:UP000033072};
RN [1] {ECO:0000313|EMBL:AKB74031.1, ECO:0000313|Proteomes:UP000033072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z-7289 {ECO:0000313|EMBL:AKB74031.1,
RC ECO:0000313|Proteomes:UP000033072};
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}.
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DR EMBL; CP009515; AKB74031.1; -; Genomic_DNA.
DR RefSeq; WP_048124816.1; NZ_CP009515.1.
DR AlphaFoldDB; A0A0E3S1S1; -.
DR STRING; 1434111.MSLAZ_0770; -.
DR GeneID; 24805474; -.
DR KEGG; mls:MSLAZ_0770; -.
DR PATRIC; fig|1434111.4.peg.969; -.
DR HOGENOM; CLU_012358_2_1_2; -.
DR OrthoDB; 372084at2157; -.
DR UniPathway; UPA00315; -.
DR Proteomes; UP000033072; Chromosome.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
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 CDD; cd01298; ATZ_TRZ_like; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01281, ECO:0000313|EMBL:AKB74031.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01281};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01281}.
FT DOMAIN 54..400
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
SQ SEQUENCE 432 AA; 46985 MW; D251EB08F728B569 CRC64;
MADIIIKNAY VLTMDPDAGD LKNGTVVIED GKITEIGDKT KESADTVIDA KGSVVMPGLV
NTHTHAAMTL LRGYADDLQL AEWLEKQIWP AEAQLKAEDV YKGSLLACLE MIKSGTTSFA
DMYFFMDETA KAVEASGLRA SLSHGLIELW NKEKGEADLK EGKRFVQTWQ GAAGGRIKTM
YGPHAPNTCS EEFLAKVKEE ARRDGVGIHI HVLETEAELN AMKKRYGKCS VHLLEDLGFL
GPDVLAAHCV WLSDGDIDIL RKRGVNVSHN PISNMKLASG IAPVYKMLEK GMNVTLGTDG
CASNNNLDLF EEMKTAALLH KVSTGNPTAL PARQVLEMAT VNGAKALGTE TGMLKVGKKA
DIIIVDMKKP HLTPCFDVPS HLVYSAKGSD VRTTIVDGKV LMDNYRVFAL DEEKVTEDAR
KAAEELVARV NA
//
