ID R7A0G9_9FIRM Unreviewed; 768 AA.
AC R7A0G9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Beta-glucosidase {ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361175};
GN ORFNames=BN699_02307 {ECO:0000313|EMBL:CDD46796.1};
OS Firmicutes bacterium CAG:534.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263027 {ECO:0000313|EMBL:CDD46796.1, ECO:0000313|Proteomes:UP000018220};
RN [1] {ECO:0000313|EMBL:CDD46796.1, ECO:0000313|Proteomes:UP000018220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:534 {ECO:0000313|Proteomes:UP000018220};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527;
CC EC=5.3.1.8; Evidence={ECO:0000256|ARBA:ARBA00000757};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|RuleBase:RU361175};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC {ECO:0000256|ARBA:ARBA00010772}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDD46796.1}.
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DR EMBL; CBHC010000074; CDD46796.1; -; Genomic_DNA.
DR AlphaFoldDB; R7A0G9; -.
DR STRING; 1263027.BN699_02307; -.
DR Proteomes; UP000018220; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:InterPro.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07010; cupin_PMI_type_I_N_bac; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR001250; Man6P_Isoase-1.
DR InterPro; IPR049071; MPI_cupin_dom.
DR InterPro; IPR046457; PMI_typeI_cat.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR NCBIfam; TIGR03356; BGL; 1.
DR NCBIfam; TIGR00218; manA; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR Pfam; PF21621; MPI_cupin_dom; 1.
DR Pfam; PF20511; PMI_typeI_cat; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CDD46796.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000018220};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 462..561
FT /note="Phosphomannose isomerase type I catalytic"
FT /evidence="ECO:0000259|Pfam:PF20511"
FT DOMAIN 697..766
FT /note="Mannose-6-phosphate isomerase cupin"
FT /evidence="ECO:0000259|Pfam:PF21621"
FT ACT_SITE 161
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 356
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 410..411
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 768 AA; 87493 MW; 96D41789625AD9BC CRC64;
MFRDDFVWGV ASSAYQIEGR EEGDGCGKNI WDTFTEQGRI LDGHSSVPAC DHMHRYKDDY
AMMRMLGIKA YRFSMSWARL IPDGTGEVNP KAVALYRDMI LEMKKNGIEP YLTMYHWEFP
QALQDRGGWL NEEAIQWFGY YAKVVAENFS DICENFITLN EPECFVGIGH LSGIHAPGLK
LPQKDVFQIA HNALRAHGQA VINLRKYACR PIKVGYAPTC GMAYPATNKP EDIEAARKVL
FGFYQPMDNW TWNVAWFNDP VFLGKYPEEG LTKFAEYLPV ITKEDMELIS QPLDFMGQNI
YNGYMVKQGA DGEPEFVGRP AGFPKTAAGW PVTPDCFYWG VKFIYDRYKL PMYITENGMS
CHDDVSLDGK VHDPNRQNFL DLYISALQKA NDEGVDLRGY FLWTFLDNFE WDKGYTERFG
IVYVDFATQK RIVKDSAYWY QKVIETNGKN LTINQKQRPI LFLNPVFKQM IWGGQKLATE
FGYAIPGDKT GECWAISAHP NGDCVIREGI YEGKTLSQLW KEEPELFGNL DLDRFPLLIK
IIDAKDDLSI QVHPNDAYAK EHENGSLGKT ECWYVLDCPE GASLVVGHNA KTREELKEMI
EQGKWSELIR EVPVQKGDFI QIDPGTVHAI KGGLMILETQ QNSDITYRVY DYDRLTDGKP
RQLHVKQSID VINVPAPSAE NSVKHMLDLP KNTLNELISC DYYTVWKLEV TEPVKVDQKH
PFMNMSVIEG EGLVNGQLVK KGDHFILPSG IGQVDLRGQM LLIASAVK
//
