MOSP_RUMA7
ID MOSP_RUMA7 Reviewed; 335 AA.
AC E6UBR9;
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=Beta-1,4-mannooligosaccharide phosphorylase;
DE EC=2.4.1.319;
DE AltName: Full=RaMP2;
GN OrderedLocusNames=Rumal_0099;
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: Catalyzes the phosphorolysis of beta-1,4-
CC mannooligosaccharides to mannose 1-phosphate (Man1P) and shorter
CC mannooligosaccharides. Can also catalyze the phosphorolysis of 4-O-
CC beta-D-mannopyranosyl-D-glucopyranose (Man-Glc), but shows higher
CC activity toward longer mannooligosaccharides. Involved in a mannan
CC catabolic pathway which feeds into glycolysis.
CC {ECO:0000269|PubMed:23093406}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-mannosyl](n) + phosphate = [(1->4)-beta-D-
CC mannosyl](n-1) + alpha-D-mannose 1-phosphate; Xref=Rhea:RHEA:45772,
CC Rhea:RHEA-COMP:11350, Rhea:RHEA-COMP:11351, ChEBI:CHEBI:27857,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58409; EC=2.4.1.319;
CC Evidence={ECO:0000269|PubMed:23093406};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28.4 mM for Man-Glc {ECO:0000269|PubMed:23093406};
CC KM=44.5 mM for beta-1,4-mannobiose {ECO:0000269|PubMed:23093406};
CC KM=7.94 mM for beta-1,4-mannotriose {ECO:0000269|PubMed:23093406};
CC KM=3.21 mM for beta-1,4-mannotetraose {ECO:0000269|PubMed:23093406};
CC KM=4.55 mM for beta-1,4-mannopentaose {ECO:0000269|PubMed:23093406};
CC Note=kcat is 20.7 sec(-1) for Man-Glc. kcat is 7.06 sec(-1) for beta-
CC 1,4-mannobiose. kcat is 27.5 sec(-1) for beta-1,4-mannotriose. kcat
CC is 33.1 sec(-1) for beta-1,4-mannotetraose. kcat is 31.9 sec(-1) for
CC beta-1,4-mannopentaose.;
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:23093406};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:23093406};
CC -!- SUBUNIT: Homohexamer in solution. {ECO:0000269|PubMed:23093406}.
CC -!- MISCELLANEOUS: Both RaMP1 (Rumal_0852) and RaMP2 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:0000305}.
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DR EMBL; CP002403; ADU20661.1; -; Genomic_DNA.
DR RefSeq; WP_013496855.1; NZ_JHYT01000018.1.
DR PDB; 5AYD; X-ray; 2.30 A; A/B/C/D/E/F=1-335.
DR PDB; 5AYE; X-ray; 2.20 A; A/B/C/D/E/F=1-335.
DR PDBsum; 5AYD; -.
DR PDBsum; 5AYE; -.
DR AlphaFoldDB; E6UBR9; -.
DR SMR; E6UBR9; -.
DR MINT; E6UBR9; -.
DR STRING; 697329.Rumal_0099; -.
DR CAZy; GH130; Glycoside Hydrolase Family 130.
DR EnsemblBacteria; ADU20661; ADU20661; Rumal_0099.
DR KEGG; ral:Rumal_0099; -.
DR eggNOG; COG2152; Bacteria.
DR HOGENOM; CLU_046648_0_0_9; -.
DR OMA; EKFYQIE; -.
DR OrthoDB; 1622507at2; -.
DR BioCyc; MetaCyc:MON-18534; -.
DR BRENDA; 2.4.1.281; 5477.
DR BRENDA; 2.4.1.319; 5477.
DR Proteomes; UP000006919; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
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..335
FT /note="Beta-1,4-mannooligosaccharide phosphorylase"
FT /id="PRO_0000421365"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:5AYD"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 44..57
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 75..87
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5AYE"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5AYE"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 124..152
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 192..210
FT /evidence="ECO:0007829|PDB:5AYE"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 233..244
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 247..257
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:5AYE"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 283..298
FT /evidence="ECO:0007829|PDB:5AYE"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:5AYE"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:5AYE"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:5AYE"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:5AYE"
SQ SEQUENCE 335 AA; 38311 MW; 0F6B3CF6A67DEC8B CRC64;
MKTQIINGVS LPNIPWQDKP ADCKDVIWRY DANPIIPRDQ LPTSNSIFNS AVVPYESEKG
KFAGVFRVDD KCRNMELHAG FSKDGIHWDI NPDRIVFEQA EKSTEEVNQW GYGYDPRVCF
IEDRFWVTWC NAYGWKPTIG VAYTFDFKTF YQCENAFLPF NRNGVLFPRK INGKYVMFSR
PSDSGHTPFG DMFISQSPDM KYWGEHRHVM GPLRAWESKK IGAGPIPIET SEGWLCFYHG
VLESCNGFVY SFSACILDKD EPWKVKYRCA EYLLSPQKIY ECVGDVQNVT FPCATLVDAD
TGRIAIYYGC ADTCVSMAFT TVDDVVDYVK SHSSV
