MGP_BACFN
ID MGP_BACFN Reviewed; 390 AA.
AC Q5LH68;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
GN OrderedLocusNames=BF0772; ORFNames=BF9343_0737;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=21539815; DOI=10.1016/j.bbrc.2011.04.095;
RA Senoura T., Ito S., Taguchi H., Higa M., Hamada S., Matsui H., Ozawa T.,
RA Jin S., Watanabe J., Wasaki J., Ito S.;
RT "New microbial mannan catabolic pathway that involves a novel
RT mannosylglucose phosphorylase.";
RL Biochem. Biophys. Res. Commun. 408:701-706(2011).
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:21539815}.
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:21539815};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.3 mM for Man-Glc {ECO:0000269|PubMed:21539815};
CC KM=2.0 mM for phosphate {ECO:0000269|PubMed:21539815};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:21539815};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:21539815};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 130 family.
CC {ECO:0000255|HAMAP-Rule:MF_00928}.
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DR EMBL; CR626927; CAH06518.1; -; Genomic_DNA.
DR RefSeq; WP_005785018.1; NC_003228.3.
DR PDB; 3WAS; X-ray; 1.50 A; A/B=1-390.
DR PDB; 3WAT; X-ray; 1.60 A; A/B=1-390.
DR PDB; 3WAU; X-ray; 1.70 A; A/B=1-390.
DR PDB; 4KMI; X-ray; 1.80 A; A/B=1-390.
DR PDBsum; 3WAS; -.
DR PDBsum; 3WAT; -.
DR PDBsum; 3WAU; -.
DR PDBsum; 4KMI; -.
DR AlphaFoldDB; Q5LH68; -.
DR SMR; Q5LH68; -.
DR STRING; 272559.BF9343_0737; -.
DR CAZy; GH130; Glycoside Hydrolase Family 130.
DR EnsemblBacteria; CAH06518; CAH06518; BF9343_0737.
DR GeneID; 66330161; -.
DR KEGG; bfs:BF9343_0737; -.
DR eggNOG; COG2152; Bacteria.
DR HOGENOM; CLU_046648_4_0_10; -.
DR OMA; KYAFYTR; -.
DR OrthoDB; 1622507at2; -.
DR BioCyc; BFRA272559:G1GHZ-806-MON; -.
DR BioCyc; MetaCyc:MON-18532; -.
DR BRENDA; 2.4.1.281; 755.
DR Proteomes; UP000006731; 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; Reference proteome; Transferase.
FT CHAIN 1..390
FT /note="4-O-beta-D-mannosyl-D-glucose phosphorylase"
FT /id="PRO_0000418860"
FT HELIX 3..20
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:3WAS"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3WAS"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:3WAS"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 68..79
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 96..108
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 163..177
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:3WAS"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 267..278
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 281..291
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:3WAS"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 321..330
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 334..342
FT /evidence="ECO:0007829|PDB:3WAS"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:3WAS"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:3WAS"
FT HELIX 354..363
FT /evidence="ECO:0007829|PDB:3WAS"
FT HELIX 371..389
FT /evidence="ECO:0007829|PDB:3WAS"
SQ SEQUENCE 390 AA; 43886 MW; 9C55CBE41B7AFEC1 CRC64;
MSLFNDKVAK LLAGHEALLM RKNEPVEEGN GVITRYRYPV LTAAHTPVFW RYDLNEETNP
FLMERIGMNA TLNAGAIKWD GKYLMLVRVE GADRKSFFAV AESPNGIDNF RFWEYPVTLP
EDVVPATNVY DMRLTAHEDG WIYGIFCAER HDDNAPIGDL SSATATAGIA RTKDLKNWER
LPDLKTKSQQ RNVVLHPEFV DGKYALYTRP QDGFIDTGSG GGIGWALIDD ITHAEVGEEK
IIDKRYYHTI KEVKNGEGPH PIKTPQGWLH LAHGVRNCAA GLRYVLYMYM TSLDDPTRLI
ASPAGYFMAP VGEERIGDVS NVLFSNGWIA DDDGKVFIYY ASSDTRMHVA TSTIERLVDY
CLHTPQDGFS SSASVEILKN LIERNLRLMK
