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DADD_METTH
ID   DADD_METTH              Reviewed;         427 AA.
AC   O27549;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=MTH_1505;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB85980.1; -; Genomic_DNA.
DR   PIR; G69067; G69067.
DR   RefSeq; WP_010877115.1; NC_000916.1.
DR   AlphaFoldDB; O27549; -.
DR   SMR; O27549; -.
DR   STRING; 187420.MTH_1505; -.
DR   EnsemblBacteria; AAB85980; AAB85980; MTH_1505.
DR   GeneID; 1471774; -.
DR   KEGG; mth:MTH_1505; -.
DR   PATRIC; fig|187420.15.peg.1468; -.
DR   HOGENOM; CLU_012358_2_1_2; -.
DR   OMA; ALIGKVC; -.
DR   UniPathway; UPA00315; -.
DR   Proteomes; UP000005223; 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; Reference proteome; Zinc.
FT   CHAIN           1..427
FT                   /note="5'-deoxyadenosine deaminase"
FT                   /id="PRO_0000122313"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ   SEQUENCE   427 AA;  46442 MW;  439527DD142182CD CRC64;
     MDNESILITG PEILDAGGIR RGSVLIEDNR IADVSNTLSP GDADTVIDGT GKLLIPGLVN
     THTHLSMTLF RGIADDLPLD RWLNDHIWPA EARLNGDYCY AGALLGCIEM IRSGTTSFND
     MYFYMDHVAR AVEEAGLRCV ISHGMIDLGD TEKMTAELRE SRRIIKECHG MADDRIRVAL
     GPHSPYTCSE ELLKETAALA DKNDLMIHIH VSETENEVSE VSRSHGMTPV EYLDEVGVLG
     PRTVAAHCVW LKDWEIDVLA ERDVKVSHNP SSNMKLASGV SPVARLLQRG VNVSLGTDGA
     ASNNNLDMFQ EMKTASLLQK VNLEDPTALP AMDVFSMATL NGARALGIDA GLIAPGKLAD
     IVILNTRRPH LTPWRNPPSH TVYSASGADV DTVICDGRIL LRDGELEVLE EKYVMELAEA
     AAAELTG
 
 
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