3OAGR_LACP7
ID 3OAGR_LACP7 Reviewed; 756 AA.
AC A9KM56;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=3-O-alpha-D-glucosyl-L-rhamnose phosphorylase;
DE EC=2.4.1.282;
DE AltName: Full=3-O-alpha-D-glucopyranosyl-L-rhamnopyranose:phosphate beta-D-glucosyltransferase;
GN OrderedLocusNames=Cphy_1019;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RX PubMed=22277537; DOI=10.1016/j.carres.2011.12.019;
RA Nihira T., Nakai H., Kitaoka M.;
RT "3-O-alpha-D-glucopyranosyl-L-rhamnose phosphorylase from Clostridium
RT phytofermentans.";
RL Carbohydr. Res. 350:94-97(2012).
CC -!- FUNCTION: Phosphorylase showing strict alpha-1,3-regioselectivity and
CC producing 3-O-alpha-D-glucopyranosyl-L-rhamnopyranose. Specific for L-
CC rhamnose as acceptor and beta-D-glucose 1-phosphate as donor. Does not
CC phosphorylate alpha,alpha-trehalose, kojibiose, nigerose, or maltose.
CC {ECO:0000269|PubMed:22277537}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-alpha-D-glucosyl-L-rhamnose + phosphate = beta-D-glucose
CC 1-phosphate + L-rhamnopyranose; Xref=Rhea:RHEA:34207,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57684, ChEBI:CHEBI:62346,
CC ChEBI:CHEBI:66909; EC=2.4.1.282;
CC Evidence={ECO:0000269|PubMed:22277537};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 mM for L-rhamnose {ECO:0000269|PubMed:22277537};
CC KM=9.6 mM for beta-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:22277537};
CC Note=kcat is 16 sec(-1) with L-rhamnose. kcat is 2.5 sec(-1) with
CC beta-D-glucose 1-phosphate.;
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:22277537};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22277537}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22277537}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR EMBL; CP000885; ABX41399.1; -; Genomic_DNA.
DR RefSeq; WP_012199045.1; NC_010001.1.
DR AlphaFoldDB; A9KM56; -.
DR SMR; A9KM56; -.
DR STRING; 357809.Cphy_1019; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR EnsemblBacteria; ABX41399; ABX41399; Cphy_1019.
DR KEGG; cpy:Cphy_1019; -.
DR eggNOG; COG1554; Bacteria.
DR HOGENOM; CLU_006285_2_1_9; -.
DR OrthoDB; 179460at2; -.
DR BioCyc; MetaCyc:MON-17154; -.
DR BRENDA; 2.4.1.282; 10424.
DR SABIO-RK; A9KM56; -.
DR Proteomes; UP000000370; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..756
FT /note="3-O-alpha-D-glucosyl-L-rhamnose phosphorylase"
FT /id="PRO_0000422596"
FT ACT_SITE 486
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 358..359
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 590..591
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ SEQUENCE 756 AA; 87991 MW; A4414F96117CAA61 CRC64;
MLIHEDNRYI VEKEYNLVTE PQNASLFTTG NGYMGVRGSL EEFGSTRIQG SFIRGFVDEI
IEVIEPFCDN EYMKKYYFDE EKLKKFDKQI SCINLVDFLL IRFRIGDEIF YPWEGEILSW
ERRLDTSQSI FQRSVTWKDK MGNITVFEFE RFASYDEEHR YCMRAMAKPQ NHFLPVEIIS
GIDTDVRTGG QRVLQFINNQ ILNNGLISCF QSGKRYGITC KIAVKNSFFM DGKLQHSIGE
QQENLLLNKA LMPGGGREYC VEKTIYLTTD RDCDPLFDTI DTVLLDVGTY DAYKEAHIRE
WSQFFSNFDI KILGDDRKDA QLRFATYHAV ITGDRNNSIH SLSAKGLTGE RYNQFVWWDC
EIYQLPIFIH AFPEVAKHAL IYRYDRLEEA RENAKLEGCK GARYPFVSSL EGKEHVWIYA
RHPFLQVHIT ADIGFGIINY FINTLDYEFM ELYGFEMLYE ICRYWVSKVI LKDGTYQLLG
VTGTDEHHPY VDNDAYTNYI VQYVLQETIL LDSQYSSTKV RDKIGITVNE LKDIEQVSRL
LYLPLEKSGL IPQFDGYFDL SRDLEVDGSG TGKNFQMKQA GLYHKSQVIK QPDVMLLFSY
LNFEIKNSRY EENWDYYEKM CESSSSLTFP VHAICSADAN RMLSFLNYFN ETVNIDLLDI
HHCAWQGVHA GCLSGAWYAI FRGLMGIVTR IDCIQINPKL IPFWQGVELS FIYQTKKIKA
TLNGNVFTLG SEDKKEISVY FQGKRYAFVD RLEVSF
