ID M0QGB7_9ACTN Unreviewed; 283 AA.
AC M0QGB7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN ORFNames=GS4_02_01380 {ECO:0000313|EMBL:GAC66427.1};
OS Gordonia soli NBRC 108243.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223545 {ECO:0000313|EMBL:GAC66427.1, ECO:0000313|Proteomes:UP000011666};
RN [1] {ECO:0000313|EMBL:GAC66427.1, ECO:0000313|Proteomes:UP000011666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108243 {ECO:0000313|EMBL:GAC66427.1,
RC ECO:0000313|Proteomes:UP000011666};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia soli NBRC 108243.";
RL Submitted (JAN-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:GAC66427.1}.
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DR EMBL; BANX01000002; GAC66427.1; -; Genomic_DNA.
DR RefSeq; WP_007616627.1; NZ_BANX01000002.1.
DR AlphaFoldDB; M0QGB7; -.
DR STRING; 1223545.GS4_02_01380; -.
DR eggNOG; COG1611; Bacteria.
DR OrthoDB; 9801098at2; -.
DR Proteomes; UP000011666; 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:UP000011666}.
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 283 AA; 31267 MW; 92F67DBEB4A2853E CRC64;
MSTDPKPTPD PHFTSDAPDP SSSGRRLPPL EDETQVCYIG ATRVHRGRDE MAQTTDRRLL
EWVDPGDDAR RSERTMRDSW RVLRIQSEFV AGFDAMSQVG QAVTVFGSAR LDPASDEYRL
AVAVGKALGE AGYAVITGGG PGAMEAANRG AWDVGAQSIG LNIELPFEQH INQWVDLGMN
FRYFFVRKTM FVKYAQAFVC LPGGFGTLDE LFEALTLVQT KKVVRFPIVL VGRDHWTGLV
DWMRDVLLAR KMISPDDLDL LHIVDDPEEA VAIITAAGQA ATR
//
