ID A0A1E4I0Y8_9PROT Unreviewed; 242 AA.
AC A0A1E4I0Y8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN ORFNames=ABS89_05475 {ECO:0000313|EMBL:ODU02753.1};
OS Thiobacillus sp. SCN 63-1177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660147 {ECO:0000313|EMBL:ODU02753.1, ECO:0000313|Proteomes:UP000094540};
RN [1] {ECO:0000313|EMBL:ODU02753.1, ECO:0000313|Proteomes:UP000094540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + H2O = adenine + D-ribose 5-phosphate;
CC Xref=Rhea:RHEA:20129, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=3.2.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000274};
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:ODU02753.1}.
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DR EMBL; MEFI01000089; ODU02753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4I0Y8; -.
DR Proteomes; UP000094540; Unassembled WGS sequence.
DR GO; GO:0008714; F:AMP nucleosidase activity; IEA:UniProtKB-EC.
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}.
SQ SEQUENCE 242 AA; 26743 MW; 93B41A7E2F95C1B7 CRC64;
MHLEKLPAAA DPGRTAEIDY SARESWRMLG IMAEFVEATE RLAFIRPAVS IFGSARTPPD
HAYYMLTEVI ARKLSDAGFS VISGGGPGIM EAANKGAYFG KSPSVGLNIQ LPHEQSANTY
QDISQTFQHF FARKVMFVKF AAAYVVMPGG YGTLDELTEA LTLVQTGKIA RIPIILVGSK
FWAGLADWVR NRLVEEGMIS PEDVDLMHII DDPEQVVDAI FGHYEKRGFI PSLAERDIQF
NL
//