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Database: UniProt
Entry: A0A1G8Q7U2_9RHOB
LinkDB: A0A1G8Q7U2_9RHOB
Original site: A0A1G8Q7U2_9RHOB 
ID   A0A1G8Q7U2_9RHOB        Unreviewed;       283 AA.
AC   A0A1G8Q7U2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE            EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN   ORFNames=SAMN04488026_101065 {ECO:0000313|EMBL:SDJ00852.1};
OS   Aliiruegeria lutimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Aliiruegeria.
OX   NCBI_TaxID=571298 {ECO:0000313|EMBL:SDJ00852.1, ECO:0000313|Proteomes:UP000199382};
RN   [1] {ECO:0000313|EMBL:SDJ00852.1, ECO:0000313|Proteomes:UP000199382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25294 {ECO:0000313|EMBL:SDJ00852.1,
RC   ECO:0000313|Proteomes:UP000199382};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNEK01000010; SDJ00852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8Q7U2; -.
DR   STRING; 571298.SAMN04488026_101065; -.
DR   OrthoDB; 9801098at2; -.
DR   Proteomes; UP000199382; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199382}.
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   283 AA;  31510 MW;  05384F1091A1C316 CRC64;
     MKDDPTKRSF RDAQEDIKTS SGVPDTEQTR SPAYRLAYDD LDFILRDQLR PVRLQLELLK
     PEIMMKEQEV ESTIVLFGGA RIRPPEEADK ALTPEMAAMS RFYVEARKFA RIMTERSIAR
     SGGREDIIIT GGGPGVMEAG NRGAADAGGK SIGLNIVLPH EQAPNAYITP ELSFNFHYFG
     VRKMHFLMRA SAIAIFPGGF GTMDELFEAL TLVQTGRMRQ VPILLFGRDF WEKVINFKAL
     AEVGTISPED LELFRVVETA EEAVAAIDSW EGVGIKRGEV PGR
//
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