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Database: UniProt
Entry: A0A2H5BBL7_9ACTN
LinkDB: A0A2H5BBL7_9ACTN
Original site: A0A2H5BBL7_9ACTN 
ID   A0A2H5BBL7_9ACTN        Unreviewed;       661 AA.
AC   A0A2H5BBL7;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   ORFNames=CFP65_7211 {ECO:0000313|EMBL:AUG81805.1};
OS   Kitasatospora sp. MMS16-BH015.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=2018025 {ECO:0000313|EMBL:AUG81805.1, ECO:0000313|Proteomes:UP000239175};
RN   [1] {ECO:0000313|EMBL:AUG81805.1, ECO:0000313|Proteomes:UP000239175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS16-BH015 {ECO:0000313|EMBL:AUG81805.1,
RC   ECO:0000313|Proteomes:UP000239175};
RA   Kim S.B., Yun B.-R.;
RT   "Genome sequence of Kitasatospora sp. MMS16-BH015.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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; CP025394; AUG81805.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H5BBL7; -.
DR   KEGG; kit:CFP65_7211; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000239175; 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:0005975; P:carbohydrate 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; 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; 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:UP000239175};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT   DOMAIN          18..384
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          395..597
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   ACT_SITE        154
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        307
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
SQ   SEQUENCE   661 AA;  72377 MW;  A8A07EC6ECA8F896 CRC64;
     MDIHRLTDRL GGLAFGGDYN PEQWDAEVWK QDDELMRLAK VNLATVGVFS WALLEPEEGR
     YDFAWLDAHL DRLHLNGVAV DLATPTASPP PWFTLAHPDA LAVRPDGLRL THGSRDTYCL
     AAPAYRQAAA RIAGALAERY GDHPALALWH VHNEYATLCW CDHTAAAFRV WLRDRHGDLD
     ALNHAWGTAF WSQHYTAWEQ ILPPRATQWH HNPGQALDFS RFWSDQTLAA YREQRDAIRA
     RSDRPVTTNL MLPGYQNLDL WAFGREVDLV SVNHYPGAPG VDAAAQAAFD ADRARSFAGG
     APWLLMESGT NTVYAGGRTL AKEPGDVLRH SLGHIARGSE GALFFQWRQS KAGAEQWHSA
     MVPHAGPDSR TFREVTALGE SLARLGELAG STVRAEVAVL HDPDAWWAMN VDGLPSAELD
     YFTALRRAHR ALWDAGATVD FAHPGQSLAG YRLVLAPALF LLTDASAENL RHYVAGGGTL
     LVQHFSGVVD EHLHSRLGGY PAAPLREALG IRVEEYRPLA EGERITLSDG STATVWSESL
     RTEGAEAVAA YTHGMLAGRP ALTRHPFGTG HGWYLSSRLD DSGYAGLVGR LLTEAGVTAG
     LPGLPPGVEA VTRHAPDGRR WHLLISHRDE AVPLPEPGRD LLTDRFLSEL PPGGCAVLRA
     H
//
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