LOGH_MYCMM
ID LOGH_MYCMM Reviewed; 187 AA.
AC B2HS63;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000250|UniProtKB:O05306};
DE EC=3.2.2.n1 {ECO:0000250|UniProtKB:O05306};
DE AltName: Full=Protein LONELY GUY homolog;
DE Short=LOG homolog;
GN OrderedLocusNames=MMAR_4233 {ECO:0000312|EMBL:ACC42641.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH AMP.
RC STRAIN=ATCC BAA-535 / M;
RG Seattle Structural Genomics Center for Infectious Disease (SSGCID);
RA Edwards T.E., Clifton M.C., Sankaran B., Moritz R.L., Johnson R.S.,
RA Stewart L.J.;
RT "Crystal structure of a putative uncharacterized protein from Mycobacterium
RT marinum bound to adenosine 5'-monophosphate AMP.";
RL Submitted (JUN-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the hydrolytic removal of ribose 5'-monophosphate
CC from nitrogen N6-modified adenosines, the final step of bioactive
CC cytokinin synthesis. {ECO:0000250|UniProtKB:O05306}.
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:0000250|UniProtKB:O05306};
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:0000250|UniProtKB:O05306};
CC -!- SIMILARITY: Belongs to the LOG family. {ECO:0000305}.
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DR EMBL; CP000854; ACC42641.1; -; Genomic_DNA.
DR RefSeq; WP_012395803.1; NC_010612.1.
DR PDB; 3SBX; X-ray; 2.50 A; A/B/C/D/E/F/G/H=2-186.
DR PDBsum; 3SBX; -.
DR AlphaFoldDB; B2HS63; -.
DR SMR; B2HS63; -.
DR STRING; 216594.MMAR_4233; -.
DR EnsemblBacteria; ACC42641; ACC42641; MMAR_4233.
DR KEGG; mmi:MMAR_4233; -.
DR eggNOG; COG1611; Bacteria.
DR HOGENOM; CLU_058336_4_0_11; -.
DR OMA; HQKPIGL; -.
DR OrthoDB; 1255127at2; -.
DR EvolutionaryTrace; B2HS63; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:0102682; F:N6-(Delta2-isopentenyl)-adenosine 5'-monophosphate phosphoribohydrolase activity; IEA:RHEA.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009691; P:cytokinin biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005269; LOG.
DR InterPro; IPR031100; LOG_fam.
DR Pfam; PF03641; Lysine_decarbox; 1.
DR TIGRFAMs; TIGR00730; TIGR00730; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokinin biosynthesis; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..187
FT /note="Cytokinin riboside 5'-monophosphate
FT phosphoribohydrolase"
FT /id="PRO_0000433001"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 98..99
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 115..121
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.2"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:3SBX"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:3SBX"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3SBX"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:3SBX"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:3SBX"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3SBX"
FT TURN 74..81
FT /evidence="ECO:0007829|PDB:3SBX"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:3SBX"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:3SBX"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:3SBX"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:3SBX"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:3SBX"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:3SBX"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:3SBX"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3SBX"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:3SBX"
SQ SEQUENCE 187 AA; 20031 MW; C749C284E3A5131D CRC64;
MTAKSDEPGR WTVAVYCAAA PTHPELLELA GAVGAAIAAR GWTLVWGGGH VSAMGAVSSA
ARAHGGWTVG VIPKMLVHRE LADHDADELV VTETMWERKQ VMEDRANAFI TLPGGVGTLD
ELLDVWTEGY LGMHDKSIVV LDPWGHFDGL RAWLSELADT GYVSRTAMER LIVVDNLDDA
LQACAPG
