ID A0A0Q7QPN4_9ACTN Unreviewed; 246 AA.
AC A0A0Q7QPN4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN ORFNames=ASD11_10535 {ECO:0000313|EMBL:KQY59934.1};
OS Aeromicrobium sp. Root495.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736550 {ECO:0000313|EMBL:KQY59934.1, ECO:0000313|Proteomes:UP000051970};
RN [1] {ECO:0000313|EMBL:KQY59934.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY59934.1,
RC ECO:0000313|Proteomes:UP000051970};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY59934.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY59934.1,
RC ECO:0000313|Proteomes:UP000051970};
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:KQY59934.1}.
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DR EMBL; LMFJ01000001; KQY59934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q7QPN4; -.
DR STRING; 1736550.ASD11_10535; -.
DR OrthoDB; 9801098at2; -.
DR Proteomes; UP000051970; 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:KQY59934.1};
KW Hydrolase {ECO:0000256|RuleBase:RU363015};
KW Reference proteome {ECO:0000313|Proteomes:UP000051970}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 246 AA; 26591 MW; 980C607C0B510C4D CRC64;
MAEGRSAVTT YNKGPVRLRG GHIPASTTDQ RLLDSDGGAD WVHTDPWRVL RIQAEFVEGF
GQLAELGPAV AVFGSARTKP DDPMYEAARQ ISAKLCERGY AVITGGGPGA MEAANRGASE
CGGVSVGLGI ELPHEQGLNE YVDMGINFRY FFVRKTMFVK YSQGYVVMPG GFGTLDELFE
ALTLAQTGKV TTFPVVLFGS AYWGGLVDWL RDTMLPDGKI SEKDLELVHV TDDVDDAVAW
FDAVAD
//