BMBP_THEPX
ID BMBP_THEPX Reviewed; 302 AA.
AC B0K2C3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Beta-1,2-mannobiose phosphorylase {ECO:0000303|PubMed:25500577};
DE EC=2.4.1.339 {ECO:0000269|PubMed:25500577};
DE AltName: Full=Beta-1,2-mannobiose:phosphate alpha-D-mannosyltransferase {ECO:0000303|PubMed:25500577};
GN OrderedLocusNames=Teth514_1789 {ECO:0000312|EMBL:ABY93074.1};
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter;
OC unclassified Thermoanaerobacter.
OX NCBI_TaxID=399726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBUNIT.
RC STRAIN=X514;
RX PubMed=25500577; DOI=10.1371/journal.pone.0114882;
RA Chiku K., Nihira T., Suzuki E., Nishimoto M., Kitaoka M., Ohtsubo K.,
RA Nakai H.;
RT "Discovery of two beta-1,2-mannoside phosphorylases showing different
RT chain-length specificities from Thermoanaerobacter sp. X-514.";
RL PLoS ONE 9:e114882-e114882(2014).
CC -!- FUNCTION: Probably involved in a salvage pathway for GDP-D-mannose
CC biosynthesis (PubMed:25500577). Catalyzes the reversible phosphorolysis
CC of 1,2-beta-oligomannan. In phosphorolytic reactions, prefers beta-1,2-
CC mannobiose (beta-1,2-Man2) as substrate. Produces alpha-D-mannose 1-
CC phosphate, which is the precursor of GDP-D-mannose (PubMed:25500577).
CC {ECO:0000269|PubMed:25500577}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-mannopyranosyl-(1->2)-D-mannopyranose + phosphate =
CC alpha-D-mannose 1-phosphate + D-mannose; Xref=Rhea:RHEA:49404,
CC ChEBI:CHEBI:4208, ChEBI:CHEBI:43474, ChEBI:CHEBI:58409,
CC ChEBI:CHEBI:62037; EC=2.4.1.339;
CC Evidence={ECO:0000269|PubMed:25500577};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49405;
CC Evidence={ECO:0000269|PubMed:25500577};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.46 mM for D-mannose (for the synthetic reaction)
CC {ECO:0000269|PubMed:25500577};
CC KM=0.69 mM for D-fructose (for the synthetic reaction)
CC {ECO:0000269|PubMed:25500577};
CC KM=1.8 mM for beta-1,2-Man2 (for the synthetic reaction)
CC {ECO:0000269|PubMed:25500577};
CC KM=2.1 mM for alpha-D-mannose 1-phosphate (for the synthetic
CC reaction) {ECO:0000269|PubMed:25500577};
CC Note=kcat is 10 sec(-1) with D-mannose as substrate (for the
CC synthetic reaction). kcat is 11 sec(-1) with D-fructose as substrate
CC (for the synthetic reaction). kcat is 7.0 sec(-1) with beta-1,2-Man2
CC as substrate (for the synthetic reaction). kcat is 12 sec(-1) with
CC alpha-D-mannose 1-phosphate as substrate (for the synthetic
CC reaction). {ECO:0000269|PubMed:25500577};
CC pH dependence:
CC Optimum pH is 6.0 for phosphorolytic activity. Optimum pH is 5.5 for
CC the synthetic reaction. {ECO:0000269|PubMed:25500577};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25500577}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 130 family.
CC {ECO:0000305}.
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DR EMBL; CP000923; ABY93074.1; -; Genomic_DNA.
DR RefSeq; WP_009052015.1; NC_010320.1.
DR PDB; 7FIP; X-ray; 2.39 A; A/B/C/D=1-302.
DR PDB; 7FIQ; X-ray; 2.22 A; A/B/C/D=1-302.
DR PDB; 7FIR; X-ray; 2.20 A; A/B/C/D=1-302.
DR PDB; 7FIS; X-ray; 2.19 A; A/B/C/D=1-302.
DR PDBsum; 7FIP; -.
DR PDBsum; 7FIQ; -.
DR PDBsum; 7FIR; -.
DR PDBsum; 7FIS; -.
DR AlphaFoldDB; B0K2C3; -.
DR SMR; B0K2C3; -.
DR CAZy; GH130; Glycoside Hydrolase Family 130.
DR EnsemblBacteria; ABY93074; ABY93074; Teth514_1789.
DR KEGG; tex:Teth514_1789; -.
DR HOGENOM; CLU_046648_0_0_9; -.
DR OMA; ARQEEPI; -.
DR BioCyc; MetaCyc:MON-19744; -.
DR UniPathway; UPA00126; -.
DR Proteomes; UP000002155; 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:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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; Glycosyltransferase; Transferase.
FT CHAIN 1..302
FT /note="Beta-1,2-mannobiose phosphorylase"
FT /id="PRO_0000452511"
SQ SEQUENCE 302 AA; 35111 MW; 76CE6C8FD9928421 CRC64;
MFRLTRLSNK PILSPIKEHE WEKEAVFNAA VIYEGNKFHL FYRASNNKFV LNTEKPEEKY
KFVSSIGYAV SEDGINFERF DKPVLVGEIP QEAWGVEDPR ITKIDNKYYM LYTGFGGRDW
LDFRICMVWS DDLKNWKGHR IVLDEPNKDA ALLSEKINGK YVLFHRRMPD IWIAYSDDLV
NWYNHKIIMS PKSHTWESKK IGIAGPPIKR EDGWLLIYHG VDNNNVYRLG VALLDLKDPS
KVIARQKEPI LEPELDWEIN GLVPNVVFSC GAVEVNDMYY VYYGAADTHI GVAVIEKEKV
KF
