BGAL_CLOP1
ID BGAL_CLOP1 Reviewed; 689 AA.
AC Q0TUR6; Q46253; Q59312;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Beta-galactosidase Pbg;
DE Short=Beta-gal {ECO:0000250|UniProtKB:Q65CX4};
DE EC=3.2.1.23;
GN Name=pbg {ECO:0000312|EMBL:BAA08485.1}; OrderedLocusNames=CPF_0160;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA08485.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A {ECO:0000312|EMBL:ABG83924.1};
RX PubMed=8577281; DOI=10.1111/j.1348-0421.1995.tb03256.x;
RA Shimizu T., Kobayashi T., Ba-Thein W., Ohtani K., Hayashi H.;
RT "Sequence analysis of flanking regions of the pfoA gene of Clostridium
RT perfringens: beta-galactosidase gene (pbg) is located in the 3'-flanking
RT region.";
RL Microbiol. Immunol. 39:677-686(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A {ECO:0000312|EMBL:ABG83924.1};
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000250|UniProtKB:Q65CX4};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08485.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D49537; BAA08485.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000246; ABG83924.1; -; Genomic_DNA.
DR RefSeq; WP_049752156.1; NC_008261.1.
DR AlphaFoldDB; Q0TUR6; -.
DR SMR; Q0TUR6; -.
DR STRING; 195103.CPF_0160; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR EnsemblBacteria; ABG83924; ABG83924; CPF_0160.
DR GeneID; 29572718; -.
DR KEGG; cpf:CPF_0160; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_1_9; -.
DR OMA; HINNEYC; -.
DR Proteomes; UP000001823; Chromosome.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR013739; Beta_galactosidase_C.
DR InterPro; IPR013738; Beta_galactosidase_Trimer.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR003476; Glyco_hydro_42.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; PTHR36447; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08533; Glyco_hydro_42C; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR PIRSF; PIRSF001084; B-galactosidase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..689
FT /note="Beta-galactosidase Pbg"
FT /id="PRO_0000407688"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT ACT_SITE 318
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 366..369
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
SQ SEQUENCE 689 AA; 79981 MW; 6034BFC444243857 CRC64;
MKNYGPISSK VTKMLHGADY NPEQWIDMPN IWGEDVRLMK LSHTNVVAVG IFSWTMLEPE
EGKFNFEWLD EIMDLMHKNG NYVILATPSG AKPIWMAHKY PETLRVAQNR VRNLYGERHN
HCYTSPIYRE KIAIIDRLLA ERYKDHPALI LWHISNEFEG QCYCPLCEEA FRDFLREKYD
NDINKLNKAW WTKFWSHTYA SFDEIEAPAP HGEPALHGLN LDWMRFVTHQ TLDYYKHERS
ILKEITPDIP VTTNFHDYIS LFRGIDYWKF APYLDVVSWD NYPYWHGERT DDHEGSRIGF
VHDLNRAILN GKPFMMMESS PSSTNWQPVA KLRRPGMHVL SSLQAVAHGS DTVQYFQWRK
SRGSSEKFHG AVVDHCGHEN TRVFRDVTKV GEILSKLDDV IGTSVEPQVA VIYDWENYWA
INDAQGPRIE QKDYFETCQK HYKAFWDMSI PTDVINMDCD FSKYKVVVAP MLYMVRPGVG
ERLEEFVKNG GTLVTTYWSG IVDENDLCFL GGFPGPLKKV TGIWAEELDA LYDEDVNYVS
VEEGNSLGMK GEYEARIFCD LIHSEGAEVL ATYKTDFYKG MPALTCNNFG EGQAYYIAFR
NNDEFLSDFY SSLAKKLTLK RAIEIDLPKG INAQVRMDEK NEFVFFMNFS SEEKTIDIKD
LDLTDMVTGE KVAKEMEIEP YGVRIVRRK
