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MTNN_BACAN
ID   MTNN_BACAN              Reviewed;         231 AA.
AC   Q81LL4; Q6HT20; Q6KMA9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE            Short=MTA/SAH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE            Short=MTAN {ECO:0000255|HAMAP-Rule:MF_01684};
DE            EC=3.2.2.9 {ECO:0000255|HAMAP-Rule:MF_01684};
DE   AltName: Full=5'-deoxyadenosine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE            Short=DOA nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE            Short=dAdo nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE   AltName: Full=5'-methylthioadenosine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE            Short=MTA nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE   AltName: Full=S-adenosylhomocysteine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE            Short=AdoHcy nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE            Short=SAH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE            Short=SRH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
GN   Name=mtnN {ECO:0000255|HAMAP-Rule:MF_01684};
GN   OrderedLocusNames=BA_4602, GBAA_4602, BAS4270;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
CC   -!- FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in
CC       both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine
CC       (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-
CC       methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves
CC       5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine
CC       (SAM) enzymes, into 5-deoxyribose and adenine. {ECO:0000255|HAMAP-
CC       Rule:MF_01684}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-
CC         ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-methyl-5'-thioadenosine = 5-(methylsulfanyl)-D-ribose
CC         + adenine; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:78440; EC=3.2.2.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5'-deoxyadenosine + H2O = 5-deoxy-D-ribose + adenine;
CC         Xref=Rhea:RHEA:29859, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:149540; EC=3.2.2.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01684};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29860;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01684};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC       pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-
CC       thioadenosine (hydrolase route): step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_01684}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01684}.
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DR   EMBL; AE016879; AAP28307.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT33723.2; -; Genomic_DNA.
DR   EMBL; AE017225; AAT56569.1; -; Genomic_DNA.
DR   RefSeq; NP_846821.1; NC_003997.3.
DR   RefSeq; WP_001217039.1; NZ_WXXJ01000027.1.
DR   RefSeq; YP_030518.1; NC_005945.1.
DR   PDB; 4QEZ; X-ray; 2.70 A; A/B/C=1-231.
DR   PDBsum; 4QEZ; -.
DR   AlphaFoldDB; Q81LL4; -.
DR   SMR; Q81LL4; -.
DR   STRING; 260799.BAS4270; -.
DR   DNASU; 1088631; -.
DR   EnsemblBacteria; AAP28307; AAP28307; BA_4602.
DR   EnsemblBacteria; AAT33723; AAT33723; GBAA_4602.
DR   GeneID; 59155057; -.
DR   GeneID; 64199717; -.
DR   KEGG; ban:BA_4602; -.
DR   KEGG; bar:GBAA_4602; -.
DR   KEGG; bat:BAS4270; -.
DR   PATRIC; fig|198094.11.peg.4569; -.
DR   eggNOG; COG0775; Bacteria.
DR   HOGENOM; CLU_031248_2_2_9; -.
DR   OMA; DQFVHSK; -.
DR   UniPathway; UPA00904; UER00871.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; Chromosome.
DR   GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1580; -; 1.
DR   HAMAP; MF_01684; Salvage_MtnN; 1.
DR   InterPro; IPR010049; MTA_SAH_Nsdase.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
DR   TIGRFAMs; TIGR01704; MTA/SAH-Nsdase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..231
FT                   /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT                   nucleosidase"
FT                   /id="PRO_0000359272"
FT   ACT_SITE        12
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT   BINDING         174..175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   HELIX           10..19
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   STRAND          21..28
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   STRAND          31..38
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   STRAND          41..47
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   HELIX           52..65
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   STRAND          89..99
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   STRAND          117..120
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   HELIX           123..132
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   STRAND          141..148
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   HELIX           156..163
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   STRAND          166..175
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   HELIX           176..186
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   STRAND          190..199
FT                   /evidence="ECO:0007829|PDB:4QEZ"
FT   HELIX           204..228
FT                   /evidence="ECO:0007829|PDB:4QEZ"
SQ   SEQUENCE   231 AA;  25255 MW;  11F3ACE054DE48AC CRC64;
     MRIAVIGAME EEVRILRDKL EQAETETVAG CEFTKGQLAG HEVILLKSGI GKVNAAMSTT
     ILLERYKPEK VINTGSAGGF HHSLNVGDVV ISTEVRHHDV DVTAFNYEYG QVPGMPPGFK
     ADEALVALAE KCMQAEENIQ VVKGMIATGD SFMSDPNRVA AIRDKFENLY AVEMEAAAVA
     QVCHQYEVPF VIIRALSDIA GKESNVSFDQ FLDQAALHST NFIVKVLEEL K
 
 
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