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LOGH_RHOFA
ID   LOGH_RHOFA              Reviewed;         198 AA.
AC   P46378;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase;
DE            EC=3.2.2.n1 {ECO:0000250|UniProtKB:O05306};
DE   AltName: Full=LOG family protein ORF6 in fasciation locus;
GN   Name=fas6;
OS   Rhodococcus fascians.
OG   Plasmid pFiD188.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1828;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=D188;
RX   PubMed=8169198; DOI=10.1128/jb.176.9.2492-2501.1994;
RA   Crespi M., Vereecke D., Temmerman W., van Montagu M., Desomer J.;
RT   "The fas operon of Rhodococcus fascians encodes new genes required for
RT   efficient fasciation of host plants.";
RL   J. Bacteriol. 176:2492-2501(1994).
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   -!- INDUCTION: During the interaction with host plants.
CC       {ECO:0000269|PubMed:8169198}.
CC   -!- MISCELLANEOUS: The FAS-operon encodes genes involved in cytokinin
CC       production and in host plant fasciation (leafy gall).
CC       {ECO:0000305|PubMed:8169198}.
CC   -!- SIMILARITY: Belongs to the LOG family. {ECO:0000305}.
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DR   EMBL; Z29635; CAA82746.1; -; Genomic_DNA.
DR   PIR; F55578; F55578.
DR   RefSeq; WP_015586136.1; NZ_NPFU01000019.1.
DR   RefSeq; YP_007878709.1; NC_021080.1.
DR   AlphaFoldDB; P46378; -.
DR   SMR; P46378; -.
DR   STRING; 1443905.GCA_000761075_00035; -.
DR   GeneID; 29801202; -.
DR   eggNOG; COG1611; Bacteria.
DR   GO; GO:0102682; F:N6-(Delta2-isopentenyl)-adenosine 5'-monophosphate phosphoribohydrolase activity; IEA:RHEA.
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   2: Evidence at transcript level;
KW   Cytokinin biosynthesis; Hydrolase; Plasmid.
FT   CHAIN           1..198
FT                   /note="Cytokinin riboside 5'-monophosphate
FT                   phosphoribohydrolase"
FT                   /id="PRO_0000087194"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
FT   BINDING         109..110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
FT   BINDING         126..132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
SQ   SEQUENCE   198 AA;  21057 MW;  597F211C65C0B2F5 CRC64;
     MNLRPMPATT VSAQARPTPK SVTVFCGAMP GRGTKYGQLA EGMGRAIARS KLRLVYGGAR
     VGLMGTLANA ALDSGGTVVG VIPESFTAIP EAAHHGLTEL HVVHDMHQRK ALMAELGDAF
     IALPGGVGTA EEFFEVLTWS HLGLHNKPCV LLNDNEYYRP LLSYIEHAAV EGFITPATRS
     RVIVCKDIEG AIAAIRSP
 
 
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