ID A0A1R3JB08_9ROSI Unreviewed; 233 AA.
AC A0A1R3JB08;
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|ARBA:ARBA00012205, ECO:0000256|RuleBase:RU363015};
DE EC=3.2.2.n1 {ECO:0000256|ARBA:ARBA00012205, ECO:0000256|RuleBase:RU363015};
GN ORFNames=COLO4_17966 {ECO:0000313|EMBL:OMO91976.1};
OS Corchorus olitorius.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=93759 {ECO:0000313|EMBL:OMO91976.1, ECO:0000313|Proteomes:UP000187203};
RN [1] {ECO:0000313|Proteomes:UP000187203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA Shommy N.S.;
RT "Corchorus olitorius genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytokinin-activating enzyme working in the direct activation
CC pathway. Phosphoribohydrolase that converts inactive cytokinin
CC nucleotides to the biologically active free-base forms.
CC {ECO:0000256|ARBA:ARBA00024884, ECO:0000256|RuleBase:RU363015}.
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|ARBA:ARBA00000881,
CC 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|ARBA:ARBA00000894,
CC ECO:0000256|RuleBase:RU363015};
CC -!- SIMILARITY: Belongs to the LOG family. {ECO:0000256|ARBA:ARBA00006763,
CC 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:OMO91976.1}.
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DR EMBL; AWUE01016403; OMO91976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3JB08; -.
DR STRING; 93759.A0A1R3JB08; -.
DR OrthoDB; 122997at2759; -.
DR Proteomes; UP000187203; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
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:SF14; CYTOKININ RIBOSIDE 5'-MONOPHOSPHATE PHOSPHORIBOHYDROLASE LOG5; 1.
DR PANTHER; PTHR31223; 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|ARBA:ARBA00022712,
KW ECO:0000256|RuleBase:RU363015}; Hydrolase {ECO:0000256|RuleBase:RU363015};
KW Reference proteome {ECO:0000313|Proteomes:UP000187203}.
SQ SEQUENCE 233 AA; 25648 MW; E23DDBB97D4E0A5E CRC64;
MDMEGKVLKS RFKRVCVFCG SSTGKRKCYR DAAVELAQEL VARRLDLVYG GGSIGLMGLV
SQAVHRAGGN VLGIIPRTLM GKEITGETVG EVRPVADMHQ RKAEMARHSD CFIALPGGYG
TLEELLEVIT WAQLGIHDKP VGLLNVDGYY NYLLTFIDKA VDDGFIKPSQ RHIIVSAPNA
KELVQKLEEY VPVHDGVIAK ASWEVELQQQ QQQQQAPQQV GFNATTLQTE IAL
//