BMAGP_BACTN
ID BMAGP_BACTN Reviewed; 322 AA.
AC Q8A8Y4;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=1,4-beta-mannosyl-N-acetylglucosamine phosphorylase {ECO:0000303|PubMed:23943617};
DE EC=2.4.1.320 {ECO:0000269|PubMed:23943617};
DE AltName: Full=4-O-beta-D-mannopyranosyl-N-acetyl-D-glucosamine:phosphate alpha-D-mannosyltransferase {ECO:0000303|PubMed:23943617};
GN OrderedLocusNames=BT_1033;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=23943617; DOI=10.1074/jbc.m113.469080;
RA Nihira T., Suzuki E., Kitaoka M., Nishimoto M., Ohtsubo K., Nakai H.;
RT "Discovery of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine phosphorylase
RT involved in the metabolism of N-glycans.";
RL J. Biol. Chem. 288:27366-27374(2013).
CC -!- FUNCTION: Involved in the N-glycan catabolism by catalyzing the
CC reversible phosphorolysis of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine
CC (ManGlcNAc) in a sequential mechanism to yield N-acetyl-D-glucosamine
CC (GlcNAc) and alpha-D-mannose 1-phosphate. It can also use beta-1,4-D-
CC mannosyl-N-acetyl-D-glucosamine-N,N-diacetylchitobiose (ManGlcNAc2) and
CC N,N-diacetylchitobiose (GlcNAc2) as substrates.
CC {ECO:0000269|PubMed:23943617}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-beta-D-mannopyranosyl-N-acetyl-D-glucosamine + phosphate =
CC alpha-D-mannose 1-phosphate + N-acetyl-D-glucosamine;
CC Xref=Rhea:RHEA:13145, ChEBI:CHEBI:43474, ChEBI:CHEBI:58409,
CC ChEBI:CHEBI:76821, ChEBI:CHEBI:506227; EC=2.4.1.320;
CC Evidence={ECO:0000269|PubMed:23943617};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 mM for ManGlcNAc (at pH 5.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:23943617};
CC KM=3.8 mM for GlcNAc (at pH 5.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:23943617};
CC KM=27 mM for GlcNAc2 (at pH 5.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:23943617};
CC Note=kcat is 37 sec(-1) for phosphorylase activity with GlcNAc (at pH
CC 5.5 and 30 degrees Celsius). kcat is 22 sec(-1) for phosphorylase
CC activity with GlcNAc2 (at pH 5.5 and 30 degrees Celsius). kcat is 210
CC sec(-1) for phosphorylase activity with ManGlcNAc (at pH 5.5 and 30
CC degrees Celsius). {ECO:0000269|PubMed:23943617};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:23943617};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23943617}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 130 family.
CC {ECO:0000305}.
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DR EMBL; AE015928; AAO76140.1; -; Genomic_DNA.
DR RefSeq; NP_809946.1; NC_004663.1.
DR RefSeq; WP_011107586.1; NZ_UYXG01000013.1.
DR AlphaFoldDB; Q8A8Y4; -.
DR SMR; Q8A8Y4; -.
DR STRING; 226186.BT_1033; -.
DR CAZy; GH130; Glycoside Hydrolase Family 130.
DR PaxDb; Q8A8Y4; -.
DR PRIDE; Q8A8Y4; -.
DR EnsemblBacteria; AAO76140; AAO76140; BT_1033.
DR GeneID; 60927008; -.
DR KEGG; bth:BT_1033; -.
DR PATRIC; fig|226186.12.peg.1050; -.
DR eggNOG; COG2152; Bacteria.
DR HOGENOM; CLU_046648_0_0_10; -.
DR InParanoid; Q8A8Y4; -.
DR OMA; KAVQMNI; -.
DR BioCyc; MetaCyc:MON-19019; -.
DR BRENDA; 2.4.1.320; 709.
DR SABIO-RK; Q8A8Y4; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; 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 Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..322
FT /note="1,4-beta-mannosyl-N-acetylglucosamine phosphorylase"
FT /id="PRO_0000430758"
SQ SEQUENCE 322 AA; 36759 MW; 266119BBF6380D1E CRC64;
MNKIQIPWEE RPVGCTDVMW RYSQNPVIGR YHIPSSNSIF NSAVVPFKDG FAGVFRCDNK
AVQMNIFTGF SKDGIHWDIS HEPIQFKAGN TEMIESEYKY DPRVTWIEDR YWVTWCNGYH
GPTIGIAYTF DFVDFFQCEN AFLPFNRNGV LFPQKIDGKY AMLSRPSDNG HTPFGDIYIS
YSPDMKYWGE HRCVMKVTPF PESAWQCTKI GAGSVPFLTD EGWLLFYHGV ITTCNGFRYA
MGSAILDKDH PEKVLYRTRE YLIGPAAPYE LQGDVPNVVF PCAALQDGER VAVYYGAADT
VVGMAFGYIQ EIIDFTKRTS II
