ID   A0A2A4TWX5_9GAMM        Unreviewed;       230 AA.
AC   A0A2A4TWX5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE            EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN   ORFNames=COB50_02900 {ECO:0000313|EMBL:PCI38048.1};
OS   Thiotrichales bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales.
OX   NCBI_TaxID=2026796 {ECO:0000313|EMBL:PCI38048.1, ECO:0000313|Proteomes:UP000218559};
RN   [1] {ECO:0000313|Proteomes:UP000218559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PCI38048.1}.
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DR   EMBL; NVTI01000043; PCI38048.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4TWX5; -.
DR   Proteomes; UP000218559; 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   230 AA;  25607 MW;  17D3A15EC62AADDE CRC64;
     MTKSNKSIPR PETPQVNDAL LVPESWKIFQ VVAEFVEGYE RLIHVKPSVS IFGSARTATT
     HPNYKMAEAI AKRLSDAGFS IVTGGGPGIM EAANKGAYAG KSLSIGLNLF IPKEQHNNKY
     QDIALNFRHF FTRKIMFVKY AAAYIVMPGG FGSLDEMMEV LTLMQTAKTH RAPMILVNKA
     YWQGLLDWFS NTLVTEGTIS KTDLDLYTLV DTTEAAVQVI TEYYKTNNLP
//