ID W0SJG7_9PROT Unreviewed; 250 AA.
AC W0SJG7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN ORFNames=SUTH_03524 {ECO:0000313|EMBL:BAO31294.1};
OS Sulfuritalea hydrogenivorans sk43H.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Sulfuritalea.
OX NCBI_TaxID=1223802 {ECO:0000313|EMBL:BAO31294.1, ECO:0000313|Proteomes:UP000031637};
RN [1] {ECO:0000313|EMBL:BAO31294.1, ECO:0000313|Proteomes:UP000031637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM22779 {ECO:0000313|EMBL:BAO31294.1};
RX PubMed=25017294; DOI=10.1016/j.syapm.2014.05.010;
RA Watanabe T., Kojima H., Fukui M.;
RT "Complete genomes of freshwater sulfur oxidizers Sulfuricella denitrificans
RT skB26 and Sulfuritalea hydrogenivorans sk43H: genetic insights into the
RT sulfur oxidation pathway of betaproteobacteria.";
RL Syst. Appl. Microbiol. 37:387-395(2014).
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}.
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DR EMBL; AP012547; BAO31294.1; -; Genomic_DNA.
DR AlphaFoldDB; W0SJG7; -.
DR STRING; 1223802.SUTH_03524; -.
DR KEGG; shd:SUTH_03524; -.
DR HOGENOM; CLU_058336_0_5_4; -.
DR OrthoDB; 9801098at2; -.
DR Proteomes; UP000031637; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031637}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 250 AA; 27535 MW; DA1EA7B818312F2D CRC64;
MNEKEKLPKS RAKGTLSLDA APARQTATSA REAWRVFGIM AEFVEATERL AEVRPAVSIF
GSARIARDSS NYQLTEKIAR LLSDAGFSVV SGGGPGVMEA ANKGAFEGKS MSIGLNIQLP
HEQKANHYQD ISQTFRHFFA RKYMFVKVAA AYVVMPGGFG TLDELLEALT LIQTGKTPRI
PLILVGTEFW AGLIDWFRAR LVAENMINPE DVDLLQVIDE PEAVVAAIFD HYEARGFGPL
PEEHELLLNL
//