DADD_METM5
ID DADD_METM5 Reviewed; 422 AA.
AC A4FW32;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=MmarC5_0086;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-2007) 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: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}.
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DR EMBL; CP000609; ABO34403.1; -; Genomic_DNA.
DR RefSeq; WP_011867864.1; NC_009135.1.
DR AlphaFoldDB; A4FW32; -.
DR SMR; A4FW32; -.
DR STRING; 402880.MmarC5_0086; -.
DR EnsemblBacteria; ABO34403; ABO34403; MmarC5_0086.
DR GeneID; 4929346; -.
DR KEGG; mmq:MmarC5_0086; -.
DR eggNOG; arCOG00695; Archaea.
DR HOGENOM; CLU_012358_2_1_2; -.
DR OMA; ALIGKVC; -.
DR OrthoDB; 40873at2157; -.
DR UniPathway; UPA00315; -.
DR Proteomes; UP000000253; 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; Zinc.
FT CHAIN 1..422
FT /note="5'-deoxyadenosine deaminase"
FT /id="PRO_0000312473"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ SEQUENCE 422 AA; 46811 MW; F7F0B74901C50B25 CRC64;
MILVKDAIIN GKKQNMLVEG NIIKKIGNIS NSEVSKDETE IIDGKNCVLI PGLINTHTHV
PMSLFRGVAD DIPLMDWLSG HIWPMESKLN EKIVYAGTLL GTIEMIKSGT TAFNDMYFFL
DSIIKAVDET GIRSTIAYGM IDLFDEEKRE KELKTARESL EMIKNLNNSR ITGALGPHAP
YTCSKEILES TNALAREFNV PIHIHMNETL DEINQVVERT GMRPFEYLNS FGFFEDVTTI
CAHCVHLSDS EIQIMKEKNM FAAHNPVSNL KLASGVSPVL KLLENNIPVT LGTDGCGSNN
NMNLFEEIKA VALIHKGVNL NPVAVTAKEA FEFGTKNGAK ALNINSGEIK EGKLADFVLI
NMKKPYLTPK ENIESHLVYS FNGVVDTVVI DGKIVLNAGK MVNIDEEKVY ELAEEAYFEL
AK
