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Database: UniProt
Entry: S3XZZ2_9MICO
LinkDB: S3XZZ2_9MICO
Original site: S3XZZ2_9MICO 
ID   S3XZZ2_9MICO            Unreviewed;       251 AA.
AC   S3XZZ2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE            EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN   ORFNames=HMPREF1484_01277 {ECO:0000313|EMBL:EPH15641.1};
OS   Dermabacter sp. HFH0086.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Dermabacter.
OX   NCBI_TaxID=1203568 {ECO:0000313|EMBL:EPH15641.1, ECO:0000313|Proteomes:UP000014577};
RN   [1] {ECO:0000313|EMBL:EPH15641.1, ECO:0000313|Proteomes:UP000014577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HFH0086 {ECO:0000313|EMBL:EPH15641.1,
RC   ECO:0000313|Proteomes:UP000014577};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Dermabacter sp. HFH0086.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-
CC         phosphate + trans-zeatin; Xref=Rhea:RHEA:48564, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16522, ChEBI:CHEBI:78346, 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-ribose 5-
CC         phosphate + N(6)-dimethylallyladenine; Xref=Rhea:RHEA:48560,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17660, ChEBI:CHEBI:57526,
CC         ChEBI:CHEBI:78346; EC=3.2.2.n1;
CC         Evidence={ECO:0000256|RuleBase:RU363015};
CC   -!- SIMILARITY: Belongs to the LOG family. {ECO:0000256|RuleBase:RU363015}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPH15641.1}.
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DR   EMBL; ATFO01000007; EPH15641.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3XZZ2; -.
DR   STRING; 1203568.HMPREF1484_01277; -.
DR   PATRIC; fig|1203568.3.peg.1252; -.
DR   eggNOG; COG1611; Bacteria.
DR   HOGENOM; CLU_058336_0_4_11; -.
DR   Proteomes; UP000014577; Unassembled WGS sequence.
DR   GO; GO:0102682; F:N6-(Delta2-isopentenyl)-adenosine 5'-monophosphate phosphoribohydrolase activity; IEA:RHEA.
DR   GO; GO:0009691; P:cytokinin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.450; -; 1.
DR   InterPro; IPR005269; LOG.
DR   InterPro; IPR031100; LOG_fam.
DR   NCBIfam; TIGR00730; Rossman fold protein, TIGR00730 family; 1.
DR   PANTHER; PTHR43393; CYTOKININ RIBOSIDE 5'-MONOPHOSPHATE PHOSPHORIBOHYDROLASE; 1.
DR   PANTHER; PTHR43393:SF2; POSSIBLE LYSINE DECARBOXYLASE; 1.
DR   Pfam; PF03641; Lysine_decarbox; 1.
DR   SUPFAM; SSF102405; MCP/YpsA-like; 1.
PE   3: Inferred from homology;
KW   Cytokinin biosynthesis {ECO:0000256|RuleBase:RU363015};
KW   Hydrolase {ECO:0000256|RuleBase:RU363015};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014577}.
SQ   SEQUENCE   251 AA;  28007 MW;  B0896F4B7B934E92 CRC64;
     MEIMKKHFHG PLSDYRKGPV FLRGKQRPTE TTDQRLLQNA GEGDWVHTDP WRVMRIQSEF
     VEGFGALAEL GPAVALFGSA RTKADHPHYA LAREVARRIG EMGLAIITGG GPGIMEAGNH
     GAIEAGTTSV GLGIELPFEQ GMNEYVELGV NFRYFFTRKT CFVKYSQAFV AFPGGFGTFD
     ELFEALCLIQ THKIKKFPLI LVGRDYWSGL VAWLEQTVQE EYGYISPGDT DLINIVDTAD
     EVIEVLKRDM K
//
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