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DADD_METMP
ID   DADD_METMP              Reviewed;         422 AA.
AC   Q6LX61;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=MMP1491;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF31047.1; -; Genomic_DNA.
DR   RefSeq; WP_011171435.1; NC_005791.1.
DR   AlphaFoldDB; Q6LX61; -.
DR   SMR; Q6LX61; -.
DR   STRING; 267377.MMP1491; -.
DR   DNASU; 2761249; -.
DR   EnsemblBacteria; CAF31047; CAF31047; MMP1491.
DR   GeneID; 2761249; -.
DR   KEGG; mmp:MMP1491; -.
DR   PATRIC; fig|267377.15.peg.1528; -.
DR   eggNOG; arCOG00695; Archaea.
DR   HOGENOM; CLU_012358_2_1_2; -.
DR   OMA; ALIGKVC; -.
DR   OrthoDB; 40873at2157; -.
DR   BioCyc; MMAR267377:MMP_RS07665-MON; -.
DR   UniPathway; UPA00315; -.
DR   Proteomes; UP000000590; 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..422
FT                   /note="5'-deoxyadenosine deaminase"
FT                   /id="PRO_0000312472"
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;  46703 MW;  031A79D45A7640DA CRC64;
     MILVKDAIIT GKKQDLLVEG NIIKKIGNIS ISEVSKDETE IIDGKNCVLI PGLINTHTHV
     PMSLFRGVAD DIPLMEWLSG HIWPMESKLN EKIVYAGTLL GTIEMIKSGT TAFNDMYFFL
     DSIIKAVDET GIRSTIAYGM IDLFDEEKRE KELKTAKESL EMIKNLNNSR ITGALGPHAP
     YTCSKEILES TNALAREYNV PIHIHMNETL DEINQVVEKT GMRPFEYLNS FGFFDNVNTI
     CAHCVHLSAS EIQIMKEKNI FAAHNPVSNL KLASGVSPVL KLLENNIPVT LGTDGCGSNN
     NMNLFEEIKA AALIHKGVNL NPVAVIAKDA FDFGTKNGAK ALNINSGEIK EGKLADFVLI
     NMKKPYLTPK ENIESHLVYS FNGVVDKVVI DGKLVLNDGK MVNIDEEKVY EIAEEAYFEL
     AN
 
 
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