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Database: UniProt
Entry: A0A0Q9M3U6_9MICO
LinkDB: A0A0Q9M3U6_9MICO
Original site: A0A0Q9M3U6_9MICO 
ID   A0A0Q9M3U6_9MICO        Unreviewed;       239 AA.
AC   A0A0Q9M3U6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE            EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN   ORFNames=ASG70_05720 {ECO:0000313|EMBL:KRE55652.1};
OS   Phycicoccus sp. Soil748.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Phycicoccus.
OX   NCBI_TaxID=1736397 {ECO:0000313|EMBL:KRE55652.1, ECO:0000313|Proteomes:UP000051855};
RN   [1] {ECO:0000313|Proteomes:UP000051855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil748 {ECO:0000313|Proteomes:UP000051855};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE55652.1, ECO:0000313|Proteomes:UP000051855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil748 {ECO:0000313|EMBL:KRE55652.1,
RC   ECO:0000313|Proteomes:UP000051855};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRE55652.1}.
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DR   EMBL; LMSC01000007; KRE55652.1; -; Genomic_DNA.
DR   RefSeq; WP_056884079.1; NZ_LMSC01000007.1.
DR   AlphaFoldDB; A0A0Q9M3U6; -.
DR   STRING; 1736397.ASG70_05720; -.
DR   Proteomes; UP000051855; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   DNA-binding {ECO:0000313|EMBL:KRE55652.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU363015}.
SQ   SEQUENCE   239 AA;  25800 MW;  EED243992B5A8F2D CRC64;
     MTLRGSRVPA STTDQRLLDS RGSTEWLHTD PWRVMRIQSE FVEGFGALAE LGPAVSVFGS
     ARTEPGTAYY ELGTELGRAL VEAGYAVITG GGPGAMEAAN RGAIEAGGAS VGLGIELPFE
     QGLNEHVNLG VNFRYFFARK TMFVKYARGF IVLPGGFGTL DELFEAVTLV QTRKVTSFPI
     VLIGTEYWGG LFDWLRGAVL EAGTVNAKDI DLLHLTDDVA EAVRIVTLAD EEVTARRPE
//
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