ID Q8XP01_CLOPE Unreviewed; 689 AA.
AC Q8XP01;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN Name=pbg {ECO:0000313|EMBL:BAB79873.1};
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB79873.1, ECO:0000313|Proteomes:UP000000818};
RN [1] {ECO:0000313|EMBL:BAB79873.1, ECO:0000313|Proteomes:UP000000818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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:0000256|ARBA:ARBA00001412,
CC ECO:0000256|PIRNR:PIRNR001084};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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DR EMBL; BA000016; BAB79873.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8XP01; -.
DR STRING; 195102.gene:10489411; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR KEGG; cpe:CPE0167; -.
DR HOGENOM; CLU_012430_1_1_9; -.
DR Proteomes; UP000000818; 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 {ECO:0000256|PIRNR:PIRNR001084};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000818};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 19..396
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 408..619
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 630..688
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 318
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 689 AA; 79993 MW; 29261E7B06B95F7E CRC64;
MKNYGPISSK VTKMLHGADY NPEQWIDMPN IWGEDVRLMK LSHTNVVAVG IFSWTMLEPE
EGKFNFEWLD EIMDLMHKNG NYVILATPSG AKPIWMAHKY PETLRVAPNR VRNLYGERHN
HCYTSPIYRE KIAIIDRLLA ERYKDHPALI LWHISNEFEG QCYCPLCEQA 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
IEEGNSLGMK GEYEARIFCD LIHSEGAEVL ATYKTDFYKG MPALTCNNFG EGQAYYIAFR
NNDEFLSDFY SSLAKKLTLK RAIEIDLPKG INAQVRMDEK NEFVFFMNFS SEEKTIDIKD
LDLTDMVTGE KVTKEMEIEP YGVRIVRRK
//
