MGP_RUMA7
ID MGP_RUMA7 Reviewed; 386 AA.
AC E6UIS7;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=4-O-beta-D-mannosyl-D-glucose phosphorylase {ECO:0000255|HAMAP-Rule:MF_00928};
DE Short=MGP {ECO:0000255|HAMAP-Rule:MF_00928};
DE Short=Mannosylglucose phosphorylase {ECO:0000255|HAMAP-Rule:MF_00928};
DE EC=2.4.1.281 {ECO:0000255|HAMAP-Rule:MF_00928};
DE AltName: Full=RaMP1;
GN OrderedLocusNames=Rumal_0852;
OS Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 /
OS 7).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=697329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7;
RX PubMed=21914885; DOI=10.1128/jb.05621-11;
RA Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., Cheng J.F.,
RA Detter C., Detter J.C., Goodwin L.A., Han C.S., Hauser L.J., Ivanova N.N.,
RA Kyrpides N.C., Land M.L., Lapidus A., Lucas S., Ovchinnikova G.,
RA Pitluck S., Tapia R., Woyke T., Boyum J., Mead D., Weimer P.J.;
RT "Complete genome of the cellulolytic ruminal bacterium Ruminococcus albus
RT 7.";
RL J. Bacteriol. 193:5574-5575(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=NE1;
RX PubMed=23093406; DOI=10.1074/jbc.m112.390336;
RA Kawahara R., Saburi W., Odaka R., Taguchi H., Ito S., Mori H., Matsui H.;
RT "Metabolic mechanism of mannan in a ruminal bacterium, Ruminococcus albus,
RT involving two mannoside phosphorylases and cellobiose 2-epimerase:
RT discovery of a new carbohydrate phosphorylase, beta-1,4-
RT mannooligosaccharide phosphorylase.";
RL J. Biol. Chem. 287:42389-42399(2012).
CC -!- FUNCTION: Converts 4-O-beta-D-mannopyranosyl-D-glucopyranose (Man-Glc)
CC to mannose 1-phosphate (Man1P) and glucose. Involved in a mannan
CC catabolic pathway which feeds into glycolysis. {ECO:0000255|HAMAP-
CC Rule:MF_00928, ECO:0000269|PubMed:23093406}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-beta-D-mannopyranosyl-D-glucopyranose + phosphate = alpha-
CC D-mannose 1-phosphate + D-glucose; Xref=Rhea:RHEA:32531,
CC ChEBI:CHEBI:4167, ChEBI:CHEBI:43474, ChEBI:CHEBI:58409,
CC ChEBI:CHEBI:64351; EC=2.4.1.281; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00928, ECO:0000269|PubMed:23093406};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.304 mM for Man-Glc {ECO:0000269|PubMed:23093406};
CC KM=5.34 mM for phosphate {ECO:0000269|PubMed:23093406};
CC KM=38.2 mM for glucose {ECO:0000269|PubMed:23093406};
CC KM=5.80 mM for Man1P {ECO:0000269|PubMed:23093406};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:23093406};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:23093406};
CC -!- SUBUNIT: Homodimer in solution. {ECO:0000269|PubMed:23093406}.
CC -!- MISCELLANEOUS: Both RaMP1 and RaMP2 (Rumal_0099) catalyze the
CC phosphorolysis of a beta-1,4-mannosidic linkage at the non-reducing end
CC of a substrate, but acceptor specificities are clearly different.
CC {ECO:0000305|PubMed:23093406}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 130 family.
CC {ECO:0000255|HAMAP-Rule:MF_00928}.
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DR EMBL; CP002403; ADU21379.1; -; Genomic_DNA.
DR RefSeq; WP_013497557.1; NZ_JHYT01000014.1.
DR PDB; 5AY9; X-ray; 2.50 A; A=1-386.
DR PDB; 5AYC; X-ray; 1.90 A; A=1-386.
DR PDBsum; 5AY9; -.
DR PDBsum; 5AYC; -.
DR AlphaFoldDB; E6UIS7; -.
DR SMR; E6UIS7; -.
DR MINT; E6UIS7; -.
DR STRING; 697329.Rumal_0852; -.
DR CAZy; GH130; Glycoside Hydrolase Family 130.
DR EnsemblBacteria; ADU21379; ADU21379; Rumal_0852.
DR KEGG; ral:Rumal_0852; -.
DR eggNOG; COG2152; Bacteria.
DR HOGENOM; CLU_046648_4_0_9; -.
DR OMA; KYAFYTR; -.
DR OrthoDB; 1622507at2; -.
DR BioCyc; MetaCyc:MON-18533; -.
DR BRENDA; 2.4.1.281; 5477.
DR Proteomes; UP000006919; Chromosome.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 2.115.10.20; -; 1.
DR HAMAP; MF_00928; Man_Glc_phosphorylase; 1.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR028583; Man_Glc_phosphorylase.
DR InterPro; IPR007184; Mannoside_phosphorylase.
DR PANTHER; PTHR34106; PTHR34106; 1.
DR Pfam; PF04041; Glyco_hydro_130; 1.
DR PIRSF; PIRSF016202; PH1107; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..386
FT /note="4-O-beta-D-mannosyl-D-glucose phosphorylase"
FT /id="PRO_0000421366"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5AY9"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5AYC"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5AYC"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:5AYC"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 94..106
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5AY9"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 140..149
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 158..175
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:5AYC"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:5AY9"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 264..275
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 278..288
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:5AYC"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 318..327
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 331..339
FT /evidence="ECO:0007829|PDB:5AYC"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:5AYC"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:5AYC"
FT HELIX 351..360
FT /evidence="ECO:0007829|PDB:5AYC"
FT HELIX 368..385
FT /evidence="ECO:0007829|PDB:5AYC"
SQ SEQUENCE 386 AA; 43646 MW; 6A5E711D3B184F8A CRC64;
MIHEKYTEMR NEQEALLSRK NTKTSFYNGI YDRYEHPVLT REHIPLHWRY DLNKETNPFF
QERLGINAVF NAGAIKLNDR YCLVARVEGN DRKSFFAVAE SDKGTEGFRF RQYPVCLPAL
TDDETNVYDM RLTQHEDGWI YGVFCVEKSA GTADLSEAVA SAGIARTKDL TNWERLPDLV
TLRSPQQRNV TLLPEFVDGK YAFYTRPMDG FIETGSGGGI GFGLADDITH AVIDEERMTS
IRRYHTITES KNGAGATPIK TERGWLNIAH GVRNTAAGLR YVIYCFVTDL SEPWKVIAEP
GGYLIAPFKD ERVGDVSNVV FTNGAIVDDN GDVYIYYASS DTRLHVAVSS IDKLLDYAFN
TPADALRTAE CVKQRCDLIK RNIELL
