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Database: UniProt
Entry: A0A0M4Q9K5_9PSEU
LinkDB: A0A0M4Q9K5_9PSEU
Original site: A0A0M4Q9K5_9PSEU 
ID   A0A0M4Q9K5_9PSEU        Unreviewed;       198 AA.
AC   A0A0M4Q9K5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE            EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN   ORFNames=WY02_21270 {ECO:0000313|EMBL:ALE80523.1};
OS   Pseudonocardia sp. AL041005-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=445576 {ECO:0000313|EMBL:ALE80523.1, ECO:0000313|Proteomes:UP000067245};
RN   [1] {ECO:0000313|EMBL:ALE80523.1, ECO:0000313|Proteomes:UP000067245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL041005-10 {ECO:0000313|EMBL:ALE80523.1,
RC   ECO:0000313|Proteomes:UP000067245};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules in
RT   bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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}.
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DR   EMBL; CP011862; ALE80523.1; -; Genomic_DNA.
DR   RefSeq; WP_062400459.1; NZ_CP011862.1.
DR   AlphaFoldDB; A0A0M4Q9K5; -.
DR   STRING; 445576.WY02_21270; -.
DR   KEGG; psea:WY02_21270; -.
DR   PATRIC; fig|445576.3.peg.4645; -.
DR   OrthoDB; 9801098at2; -.
DR   Proteomes; UP000067245; Chromosome.
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; PTHR31223; LOG FAMILY PROTEIN YJL055W; 1.
DR   PANTHER; PTHR31223:SF11; LOG FAMILY PROTEIN YJL055W; 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}.
SQ   SEQUENCE   198 AA;  20821 MW;  71196CF45DCFF0D2 CRC64;
     MAGPEPGFAV CVYCASSDGV APHYLDLARE VGRAVAARGW TLVSGGGRKS MMGAVAAGAR
     EAGGRTVGVI PRSMVEREWA DHDSDELLVV ESMRERKQQM EDRADAFLAL PGGIGTCEEL
     FEVWTAGSLG LHGKPVVLLD PDGHWDGLVD WVAGLADRGF ASRGPIERLR QVRGDDSAPA
     DPAGLAGAAL DECARPLT
//
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