(data stored in SCRATCH3701 zone)

SWISSPROT: D5EA47_METMS

ID   D5EA47_METMS            Unreviewed;       444 AA.
AC   D5EA47;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 56.
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   OrderedLocusNames=Mmah_0521 {ECO:0000313|EMBL:ADE36048.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE36048.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE36048.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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; CP001994; ADE36048.1; -; Genomic_DNA.
DR   RefSeq; WP_013036991.1; NC_014002.1.
DR   EnsemblBacteria; ADE36048; ADE36048; Mmah_0521.
DR   GeneID; 8982662; -.
DR   KEGG; mmh:Mmah_0521; -.
DR   eggNOG; arCOG00695; Archaea.
DR   eggNOG; COG0402; LUCA.
DR   HOGENOM; HOG000250646; -.
DR   KO; K12960; -.
DR   OMA; ASYFATN; -.
DR   OrthoDB; 40873at2157; -.
DR   BioCyc; MMAH547558:G1GHT-523-MONOMER; -.
DR   UniPathway; UPA00315; -.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0090613; F:5'-deoxyadenosine deaminase activity; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; D5EA47.
DR   SWISS-2DPAGE; D5EA47.
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01281, ECO:0000313|EMBL:ADE36048.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01281};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01281}.
FT   DOMAIN          54..400
FT                   /note="Amidohydro-rel"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   METAL           63
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   METAL           65
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   METAL           211
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   METAL           299
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         92
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         154
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         184
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         214
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
FT   BINDING         299
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01281"
SQ   SEQUENCE   444 AA;  48491 MW;  3DCD9F3774D30834 CRC64;
     MADILIKNGY ILTMDPDTGD LKKGEVAIEN GRIIYVGLSY NGKADKIIDA SGSVVMPGLV
     NTHNHAGMTL LRGYADDLPL AEWLEDYIWP VEEKLGPEEI YAGVRLACLE MIKSGTTTFA
     DMYIHEQAAA RAVEDCGMRA ALSYGMIDFG DPQRAESSLL KGRNFVKDFN GAANGRISAM
     YGPHAPHTCS QQFLQDVRKQ ARKDDVKVHI HVLETEAELN QMKEKYGKCS VNMLHDIGFF
     DSDVLAAHCI WLSEGDMNIL AETGVHVSHD PVSNMKTAAG IAPVPQLLEK GVNVSLSTDG
     CASNNNLDMF GVMKTAALLH KVNSMDLTVI DARKVLEMAT VYGAKALGIE AGMIKEGYYG
     DLIVVDMKRP HLTPLYDVDS HLVYSARGSD VTTVLVDGKV LMENGKVLCM DEYEIMMEAS
     KAAKKTDSQH LIDVLGLNDP SVDQ
//

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