BOLMP_THEPX
ID BOLMP_THEPX Reviewed; 296 AA.
AC B0K2C2;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=1,2-beta-oligomannan phosphorylase {ECO:0000303|PubMed:25500577};
DE EC=2.4.1.340 {ECO:0000269|PubMed:25500577};
DE AltName: Full=1,2-beta-oligomannan:phosphate alpha-D-mannosyltransferase {ECO:0000303|PubMed:25500577};
GN OrderedLocusNames=Teth514_1788 {ECO:0000312|EMBL:ABY93073.1};
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 1,2-beta-
CC oligomannan with a degree of polymerization (DP) of 3, 4 and 5.
CC Produces alpha-D-mannose 1-phosphate, which is the precursor of GDP-D-
CC mannose (PubMed:25500577). {ECO:0000269|PubMed:25500577}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->2)-beta-D-mannosyl](n) + phosphate = [(1->2)-beta-D-
CC mannosyl](n-1) + alpha-D-mannose 1-phosphate; Xref=Rhea:RHEA:49408,
CC Rhea:RHEA-COMP:12390, Rhea:RHEA-COMP:12391, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58409, ChEBI:CHEBI:59573; EC=2.4.1.340;
CC Evidence={ECO:0000269|PubMed:25500577};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49409;
CC Evidence={ECO:0000269|PubMed:25500577};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.41 mM for D-mannose (for the synthetic reaction)
CC {ECO:0000269|PubMed:25500577};
CC KM=0.20 mM for D-fructose (for the synthetic reaction)
CC {ECO:0000269|PubMed:25500577};
CC KM=0.77 mM for beta-1,2-mannobiose (beta-1,2-Man2) (for the synthetic
CC reaction) {ECO:0000269|PubMed:25500577};
CC KM=1.2 mM for beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-
CC (1->2)-D-mannose (beta-1,2-Man3) (for the synthetic reaction)
CC {ECO:0000269|PubMed:25500577};
CC KM=1.4 mM for alpha-D-mannose 1-phosphate (for the synthetic
CC reaction) {ECO:0000269|PubMed:25500577};
CC Note=kcat is 1.9 sec(-1) with D-mannose as substrate (for the
CC synthetic reaction). kcat is 2.0 sec(-1) with D-fructose as substrate
CC (for the synthetic reaction). kcat is 25 sec(-1) with beta-1,2-Man2
CC as substrate (for the synthetic reaction). kcat is 43 sec(-1) with
CC beta-1,2-Man3 as substrate (for the synthetic reaction). kcat is 22
CC sec(-1) with alpha-D-mannose 1-phosphate as substrate (for the
CC synthetic reaction). {ECO:0000269|PubMed:25500577};
CC pH dependence:
CC Optimum pH is 6.0 for phosphorolytic activity. Optimum pH is 5.0 for
CC the synthetic reaction. {ECO:0000269|PubMed:25500577};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25500577}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 130 family.
CC {ECO:0000305}.
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DR EMBL; CP000923; ABY93073.1; -; Genomic_DNA.
DR RefSeq; WP_009052014.1; NC_010320.1.
DR AlphaFoldDB; B0K2C2; -.
DR SMR; B0K2C2; -.
DR CAZy; GH130; Glycoside Hydrolase Family 130.
DR EnsemblBacteria; ABY93073; ABY93073; Teth514_1788.
DR KEGG; tex:Teth514_1788; -.
DR HOGENOM; CLU_046648_0_0_9; -.
DR OMA; WLVIYHA; -.
DR BioCyc; MetaCyc:MON-19745; -.
DR BRENDA; 2.4.1.340; 5468.
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 Carbohydrate metabolism; Glycosyltransferase; Transferase.
FT CHAIN 1..296
FT /note="1,2-beta-oligomannan phosphorylase"
FT /id="PRO_0000452512"
SQ SEQUENCE 296 AA; 33997 MW; CF1C287BB2D45C35 CRC64;
MIKLKRLSDK PVLMPKAENE WERAAVFNTA AIYDNGLFHL IYRATDIGPH AKYGKYISRL
GYAVSKDGIN FMRLDKPVMS NETEQELRGL EDPRIVKIDG IYYMMYTGFG DRFQDDYRIC
LATSKNLIDW ERKGVVLDEP NKDASLFPEK INGKYVMLHR RYPDIWIAFS DDLKNWYDHK
PILKPIPNTW ESARVGIGGP PIKTKDGWFL IYHAADDNNV YRLGAVLLDL EDPSKVIARQ
KEPILEPELG WEKEGYIPNV VFSCGNAVKD DTIYVYYGGA DTVIGVAILE MKDIKF
