位置:首页 > 蛋白库 > DADD_METHJ
DADD_METHJ
ID   DADD_METHJ              Reviewed;         449 AA.
AC   Q2FRU6;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Mhun_2445;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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}.
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; CP000254; ABD42146.1; -; Genomic_DNA.
DR   RefSeq; WP_011449404.1; NC_007796.1.
DR   AlphaFoldDB; Q2FRU6; -.
DR   SMR; Q2FRU6; -.
DR   STRING; 323259.Mhun_2445; -.
DR   EnsemblBacteria; ABD42146; ABD42146; Mhun_2445.
DR   GeneID; 3922433; -.
DR   KEGG; mhu:Mhun_2445; -.
DR   eggNOG; arCOG00695; Archaea.
DR   HOGENOM; CLU_012358_2_1_2; -.
DR   OMA; ALIGKVC; -.
DR   OrthoDB; 40873at2157; -.
DR   UniPathway; UPA00315; -.
DR   Proteomes; UP000001941; 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; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..449
FT                   /note="5'-deoxyadenosine deaminase"
FT                   /id="PRO_0000312483"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ   SEQUENCE   449 AA;  49429 MW;  36048BEDCABA03FD CRC64;
     MADPKDISPC KNEDLFLKCR STLITGVLLP DKTRSDIWYD ETGTIRTCGP DIARNHRNEA
     DIILDGSGFL AMPGLINTHT HAAMTLLRGY ADDMHLQQWL SEKIWPLEAH LTGEHVYWGT
     KLACLEMIRS GTIAFNDMYF YMKDAARAVQ ESGIRAVLSH GIITFGDEAK MEAELKATED
     LVHHVRSLNT SLITSAIAPH APYTVPPQHL EVCADYSQKE KIIIHTHLAE TKQEVDDCQK
     SYGMTPAALL DKTGCLTERT VAAHGCWLSE DDCRLLAERR VSVAHNPVSN MKLATGRAMP
     YHWLKDQGVN VCLGTDGCSS NNNLDMLEEM KTAALCQKFF WNSDTLLPAA EALSMGTSWG
     AKALGYQGGV IQEGMPADIV LISLSHPSMV PLHNPVSNIA YSAEGSVVDT VICQGKILMY
     NRYIPDEEKI IAGARESADD LLNRAGIMA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024