BMBP_LISIN
ID BMBP_LISIN Reviewed; 355 AA.
AC Q92DF6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Beta-1,2-mannobiose phosphorylase {ECO:0000303|PubMed:26632508};
DE EC=2.4.1.339 {ECO:0000269|PubMed:26632508};
GN OrderedLocusNames=lin0857 {ECO:0000312|EMBL:CAC96089.1};
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2] {ECO:0007744|PDB:5B0P, ECO:0007744|PDB:5B0Q, ECO:0007744|PDB:5B0R, ECO:0007744|PDB:5B0S}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP MANNOSE; BETA-1,2-MANNOBIOSE AND BETA-1,2-MANNOTRIOSE, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=26632508; DOI=10.1016/j.febslet.2015.11.034;
RA Tsuda T., Nihira T., Chiku K., Suzuki E., Arakawa T., Nishimoto M.,
RA Kitaoka M., Nakai H., Fushinobu S.;
RT "Characterization and crystal structure determination of beta-1,2-
RT mannobiose phosphorylase from Listeria innocua.";
RL FEBS Lett. 589:3816-3821(2015).
CC -!- FUNCTION: Catalyzes the reversible phosphorolysis of 1,2-beta-
CC oligomannan (PubMed:26632508). In phosphorolytic reactions, prefers
CC beta-1,2-mannobiose (beta-1,2-Man2) as substrate, but can also use
CC beta-1,2-mannotriose (PubMed:26632508). {ECO:0000269|PubMed:26632508}.
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:26632508};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 mM for D-mannose (for the synthetic reaction)
CC {ECO:0000269|PubMed:26632508};
CC KM=1.5 mM for D-fructose (for the synthetic reaction)
CC {ECO:0000269|PubMed:26632508};
CC KM=5.1 mM for beta-1,2-Man2 (for the synthetic reaction)
CC {ECO:0000269|PubMed:26632508};
CC KM=3.1 mM for alpha-D-mannose 1-phosphate (for the synthetic
CC reaction) {ECO:0000269|PubMed:26632508};
CC Note=kcat is 31 sec(-1) with D-mannose as substrate (for the
CC synthetic reaction). kcat is 3.9 sec(-1) with D-fructose as substrate
CC (for the synthetic reaction). kcat is 12 sec(-1) with beta-1,2-Man2
CC as substrate (for the synthetic reaction). kcat is 33 sec(-1) with
CC alpha-D-mannose 1-phosphate as substrate (for the synthetic
CC reaction). kcat is 35 sec(-1) with beta-1,2-Man2 as substrate (for
CC the phosphorolytic reaction). kcat is 12 sec(-1) with beta-1,2-
CC mannotriose as substrate (for the phosphorolytic reaction).
CC {ECO:0000269|PubMed:26632508};
CC pH dependence:
CC Optimum pH is 7.0 for phosphorolytic activity. Optimum pH is 6.0 for
CC the synthetic reaction. {ECO:0000269|PubMed:26632508};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26632508}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 130 family.
CC {ECO:0000305}.
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DR EMBL; AL596166; CAC96089.1; -; Genomic_DNA.
DR PIR; AI1539; AI1539.
DR RefSeq; WP_003761245.1; NC_003212.1.
DR PDB; 5B0P; X-ray; 1.90 A; A/B=1-355.
DR PDB; 5B0Q; X-ray; 2.30 A; A/B=1-355.
DR PDB; 5B0R; X-ray; 1.80 A; A/B=1-355.
DR PDB; 5B0S; X-ray; 2.10 A; A/B=1-355.
DR PDBsum; 5B0P; -.
DR PDBsum; 5B0Q; -.
DR PDBsum; 5B0R; -.
DR PDBsum; 5B0S; -.
DR AlphaFoldDB; Q92DF6; -.
DR SMR; Q92DF6; -.
DR MINT; Q92DF6; -.
DR STRING; 272626.lin0857; -.
DR CAZy; GH130; Glycoside Hydrolase Family 130.
DR EnsemblBacteria; CAC96089; CAC96089; CAC96089.
DR KEGG; lin:lin0857; -.
DR eggNOG; COG2152; Bacteria.
DR HOGENOM; CLU_046648_0_0_9; -.
DR OMA; KYYMIWG; -.
DR OrthoDB; 1622507at2; -.
DR BRENDA; 2.4.1.339; 3044.
DR Proteomes; UP000002513; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; 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; Glycosyltransferase; Transferase.
FT CHAIN 1..355
FT /note="Beta-1,2-mannobiose phosphorylase"
FT /id="PRO_0000452510"
FT BINDING 31
FT /ligand="beta-D-Manp-(1->2)-beta-D-Manp-(1->2)-D-Manp"
FT /ligand_id="ChEBI:CHEBI:131448"
FT /evidence="ECO:0000269|PubMed:26632508,
FT ECO:0007744|PDB:5B0S"
FT BINDING 46
FT /ligand="beta-D-Manp-(1->2)-beta-D-Manp-(1->2)-D-Manp"
FT /ligand_id="ChEBI:CHEBI:131448"
FT /evidence="ECO:0000269|PubMed:26632508,
FT ECO:0007744|PDB:5B0S"
FT BINDING 89
FT /ligand="beta-D-Manp-(1->2)-beta-D-Manp-(1->2)-D-Manp"
FT /ligand_id="ChEBI:CHEBI:131448"
FT /evidence="ECO:0000269|PubMed:26632508,
FT ECO:0007744|PDB:5B0S"
FT BINDING 140..141
FT /ligand="beta-D-Manp-(1->2)-beta-D-Manp-(1->2)-D-Manp"
FT /ligand_id="ChEBI:CHEBI:131448"
FT /evidence="ECO:0000269|PubMed:26632508,
FT ECO:0007744|PDB:5B0S"
FT BINDING 188
FT /ligand="beta-D-Manp-(1->2)-beta-D-Manp-(1->2)-D-Manp"
FT /ligand_id="ChEBI:CHEBI:131448"
FT /evidence="ECO:0000269|PubMed:26632508,
FT ECO:0007744|PDB:5B0S"
FT BINDING 273
FT /ligand="beta-D-Manp-(1->2)-beta-D-Manp-(1->2)-D-Manp"
FT /ligand_id="ChEBI:CHEBI:131448"
FT /evidence="ECO:0000269|PubMed:26632508,
FT ECO:0007744|PDB:5B0S"
FT BINDING 333
FT /ligand="beta-D-Manp-(1->2)-beta-D-Manp-(1->2)-D-Manp"
FT /ligand_id="ChEBI:CHEBI:131448"
FT /evidence="ECO:0000269|PubMed:26632508,
FT ECO:0007744|PDB:5B0S"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5B0R"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 24..37
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 40..51
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:5B0R"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:5B0R"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5B0Q"
FT STRAND 101..119
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 162..175
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 217..235
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:5B0R"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:5B0P"
FT STRAND 311..321
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:5B0R"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:5B0R"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:5B0R"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:5B0R"
SQ SEQUENCE 355 AA; 39995 MW; 2C831C751ABCA4FB CRC64;
MNIYRYEENP LITPLDVKPI HEGFEVIGAF NGGVAEYNGE VLLLLRVAEK PVSEDPEIVL
APVYNAKNKE LELQSFRLDD ENYDFEDPRM IRSKAKLEGF SYLTSLSYIR IARSKDGHHF
TLDEKPFLYP FNEYQTFGIE DARVTQIGDT YHVNFSAVSE FGVADALVTT KDFENLEYQG
NIFAPENKDV LIFPEKINGK YYALHRPSLK SIGNLDIWIA SSPDLRSFGD HRHLLGIRPG
EYDSGRVGGG CVPIKTEEGW LILYHGATEE NRYVMGAALL DLNDPTIVLK RTKTPILEPV
ADYEKNGFFG DVVFACGAIQ EGDTLHMYYG VADTSMAGCD MKISEILHQL EVEAK
