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   27-MAR-2024, entry version 94.
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; Bacillota; 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
RC   107 / 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
RC   107 / 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   PaxDb; 195103-CPF_0160; -.
DR   KEGG; cpf:CPF_0160; -.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_012430_1_1_9; -.
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   CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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; BETA-GALACTOSIDASE GANA; 1.
DR   PANTHER; PTHR36447:SF1; BETA-GALACTOSIDASE GANA; 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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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
//