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Database: UniProt
Entry: A0A1Q4XGW3_9PSEU
LinkDB: A0A1Q4XGW3_9PSEU
Original site: A0A1Q4XGW3_9PSEU 
ID   A0A1Q4XGW3_9PSEU        Unreviewed;       254 AA.
AC   A0A1Q4XGW3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE            EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN   ORFNames=A6A25_09880 {ECO:0000313|EMBL:OKI21586.1};
OS   Saccharothrix sp. CB00851.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1835005 {ECO:0000313|EMBL:OKI21586.1, ECO:0000313|Proteomes:UP000186828};
RN   [1] {ECO:0000313|EMBL:OKI21586.1, ECO:0000313|Proteomes:UP000186828}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB00851 {ECO:0000313|EMBL:OKI21586.1,
RC   ECO:0000313|Proteomes:UP000186828};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKI21586.1}.
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DR   EMBL; LWLC01000034; OKI21586.1; -; Genomic_DNA.
DR   RefSeq; WP_073895921.1; NZ_LWLC01000034.1.
DR   AlphaFoldDB; A0A1Q4XGW3; -.
DR   STRING; 1835005.A6A25_09880; -.
DR   Proteomes; UP000186828; 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:UP000186828}.
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   254 AA;  28014 MW;  D920E9E94F8D4266 CRC64;
     MTDSVDEHPK EKQRGPVVLR RGRRDELTTT DQRLLDSRGP SDWVHTDPWR VLRIQAEFVE
     GFGALAEVPS AVTVFGSART GRDHPEYEIG RKLGGALAEA GFAVITGGGP GAMEAVNRGC
     SEAGGFSVGL GIELPFEQGL NPWVDLGVNF RYFFVRKTMF IKYSQAFICL PGGFGTLDEL
     FEALTLVQTK KVTKFPVVLF GKAYWQGLYD WVRDSVLASG KVSEKDLDLL HLTDDIDDAV
     RVVNDAHKAW ADAH
//
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