(data stored in ACNUC7421 zone)

SWISSPROT: D6XY43_BACIE

ID   D6XY43_BACIE            Unreviewed;       452 AA.
AC   D6XY43;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=5-methylthioadenosine/S-adenosylhomocysteine deaminase {ECO:0000256|HAMAP-Rule:MF_01281};
DE            Short=MTA/SAH deaminase {ECO:0000256|HAMAP-Rule:MF_01281};
DE            EC=3.5.4.28 {ECO:0000256|HAMAP-Rule:MF_01281};
DE            EC=3.5.4.31 {ECO:0000256|HAMAP-Rule:MF_01281};
GN   Name=mtaD {ECO:0000256|HAMAP-Rule:MF_01281};
GN   OrderedLocusNames=Bsel_0580 {ECO:0000313|EMBL:ADH98116.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98116.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98116.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the deamination of 5-methylthioadenosine and
CC       S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-
CC       homocysteine, respectively. Is also able to deaminate adenosine.
CC       {ECO:0000256|HAMAP-Rule:MF_01281}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-
CC         inosyl-L-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-
CC         methyl-5'-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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01281};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01281};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. MTA/SAH deaminase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01281}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01281}.
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DR   EMBL; CP001791; ADH98116.1; -; Genomic_DNA.
DR   RefSeq; WP_013171545.1; NC_014219.1.
DR   STRING; 439292.Bsel_0580; -.
DR   EnsemblBacteria; ADH98116; ADH98116; Bsel_0580.
DR   KEGG; bse:Bsel_0580; -.
DR   eggNOG; ENOG4105D6T; Bacteria.
DR   eggNOG; COG0402; LUCA.
DR   HOGENOM; HOG000250646; -.
DR   OMA; IIASWGK; -.
DR   OrthoDB; 1592010at2; -.
DR   BioCyc; BSEL439292:G1GLR-623-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0090614; F:5'-methylthioadenosine 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-UniRule.
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; D6XY43.
DR   SWISS-2DPAGE; D6XY43.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01281,
KW   ECO:0000313|EMBL:ADH98116.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01281};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01281}.
FT   DOMAIN       54    412       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   METAL        63     63       Zinc; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01281}.
FT   METAL        65     65       Zinc; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01281}.
FT   METAL       219    219       Zinc; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01281}.
FT   METAL       307    307       Zinc. {ECO:0000256|HAMAP-Rule:MF_01281}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01281}.
FT   BINDING     222    222       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01281}.
FT   BINDING     307    307       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01281}.
SQ   SEQUENCE   452 AA;  49701 MW;  4FD3E60073E9034B CRC64;
     MGSIVLKNAE IITMNAGREA VFGDVLIEGD TITAVGKNLP CPDDAEVIDA TGRVVIPGFI
     QTHIHLCQTL FRGRGDDLEL MDWLKGRIWP LEAAHDEESI YYSALLGTGE LIQSGTTSIV
     DMETVHHTDS AFEGMAQSGI RAISGKVMMD KGDEVPLPLQ EKTAESLQAS QDLYEKWHGY
     DNGRLQYAYS PRFVVSCTEE LLRETARLSE MQNVRVHTHA AENRGEIAIV ERETGMRNVE
     YLHKLGLANE RLMLAHCIWL SDNEKKIIRD NRVNVTHCPG SNLKLASGKA EIPQLLDAHV
     CVSLGADGAP CNNNLDMFNE MRLAALIHKP EHGPTAMDAK TVFEMATIGG AKAMGLDDKI
     GSIEPGKKAD LAILNLNDLH MYPSYGVDTL SRIVYSATRA DVETTIINGK PVMKNRMLHT
     MDKETLMQEA NTSIKRLIKR SGIPGQTKAV SG
//

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