(data stored in ACNUC7421 zone)

SWISSPROT: Q47SN3_THEFY

ID   Q47SN3_THEFY            Unreviewed;       269 AA.
AC   Q47SN3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE            EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN   OrderedLocusNames=Tfu_0496 {ECO:0000313|EMBL:AAZ54534.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54534.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-
CC         phosphate + trans-zeatin; Xref=Rhea:RHEA:48564,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16522, ChEBI:CHEBI:78346,
CC         ChEBI:CHEBI:87947; EC=3.2.2.n1;
CC         Evidence={ECO:0000256|RuleBase:RU363015};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-(dimethylallyl)adenosine 5'-phosphate = D-
CC         ribose 5-phosphate + N(6)-dimethylallyladenine;
CC         Xref=Rhea:RHEA:48560, ChEBI:CHEBI:15377, ChEBI:CHEBI:17660,
CC         ChEBI:CHEBI:57526, ChEBI:CHEBI:78346; EC=3.2.2.n1;
CC         Evidence={ECO:0000256|RuleBase:RU363015};
CC   -!- SIMILARITY: Belongs to the LOG family.
CC       {ECO:0000256|RuleBase:RU363015}.
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DR   EMBL; CP000088; AAZ54534.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0496; -.
DR   EnsemblBacteria; AAZ54534; AAZ54534; Tfu_0496.
DR   KEGG; tfu:Tfu_0496; -.
DR   eggNOG; ENOG4105CNZ; Bacteria.
DR   eggNOG; COG1611; LUCA.
DR   HOGENOM; HOG000156897; -.
DR   OMA; PWRVMRI; -.
DR   BioCyc; TFUS269800:G1G4Q-505-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009691; P:cytokinin biosynthetic process; IEA:UniProtKB-UniRule.
DR   InterPro; IPR005269; LOG.
DR   InterPro; IPR031100; LOG_fam.
DR   Pfam; PF03641; Lysine_decarbox; 1.
DR   TIGRFAMs; TIGR00730; TIGR00730; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47SN3.
DR   SWISS-2DPAGE; Q47SN3.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytokinin biosynthesis {ECO:0000256|RuleBase:RU363015};
KW   Hydrolase {ECO:0000256|RuleBase:RU363015};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   COILED      236    269       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   269 AA;  29953 MW;  A604598C1274A53A CRC64;
     MTDSRSIERQ AGPLTYRGRE IPKSTTDQRL LDRRGPTDWV HTDPWRVLRI QSEFVEGFGM
     LSEVGRAVCV FGSARIKPET PYYELGEEIG RKLVEAGYTV ITGGGPGLME AANKGAADVG
     GTSIGLGIEL PFEQSLNDYV NLGVVFRYFF VRKTMFVKYS QAFVVLPGGF GTLDELFEAL
     TLVQTGKITR FPVILVGTDF WGGLVEWIND RLLAEGLISP SDPDLIHLTD DPDDVIETIQ
     RAHAEWERAL EEEEAVTELE EALREAEHS
//

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