ID   A0A089KSJ8_9BACL        Unreviewed;       667 AA.
AC   A0A089KSJ8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=R70331_12030 {ECO:0000313|EMBL:AIQ52161.1};
OS   Paenibacillus sp. FSL R7-0331.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ52161.1, ECO:0000313|Proteomes:UP000029487};
RN   [1] {ECO:0000313|EMBL:AIQ52161.1, ECO:0000313|Proteomes:UP000029487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ52161.1,
RC   ECO:0000313|Proteomes:UP000029487};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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; CP009284; AIQ52161.1; -; Genomic_DNA.
DR   RefSeq; WP_042175554.1; NZ_CP009284.1.
DR   AlphaFoldDB; A0A089KSJ8; -.
DR   STRING; 1536773.R70331_12030; -.
DR   KEGG; paee:R70331_12030; -.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_012430_2_0_9; -.
DR   Proteomes; UP000029487; 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: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   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; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR   PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 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   Reference proteome {ECO:0000313|Proteomes:UP000029487}.
FT   DOMAIN          10..376
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          391..594
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   ACT_SITE        144
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        303
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   667 AA;  74902 MW;  278D0FBDFA21888D CRC64;
     MDKLLYGVAY YDEYMPYERL AEDIRMMKEA GINTVRIAES TWSTHEPQNG VFDFTSVDRV
     LDAMHEAGIH VIVGTPTYAI PAWMVKEHPD VLAVTSAGRG KYGARQIMDI THPVYLFYAE
     RIIRKLLERV HKHPAVIGYQ TDNETKHYET AGDNVQLKFV KYMRKTYGTL EKINHQFGLD
     YWSNRIDSWE DFPSVAGTIN GSLGAEFARF QRGLVNDFLA WQVAIVNEYK QPGQFVTQNF
     DYEWRGYSFG VQPSVDHFAA AEPFDIAGVD IYHPSQSELT GAEIAFGGDI SRSVKRSNYL
     VLETQAQAFP QWTPYPGQLR LLAFSHIGSG ANMVAYWHWH SIHNSFETYW KGLLSHDFLP
     NPVYKEACTI GADFKRLSPQ LTGLVKKNKI AFMISNEALS AMEWFKLPDG KNYNDVVRWL
     YDEFYRMNAE CDFIQPSSPY LHEYDLVVVP ALYAVSDEAL LALNEYVKGC GHVLYSFKSG
     FADEQVKVRT VQQPGILSEA CGIGYSMFVT PDAETGLTGG LFPEGGAGTV NSWMELLVPG
     TAEVLAFYDH PEWGNYAAAT RNTFGEGTAT YVGCMMDASD LAVIVRDTLQ TAGLWTEQQE
     YAFPLIVKSA TTREGTPVRF YYNYSGKQLA GVRPVKGGTE LLSGSAVSVD GELELAPWGV
     QIILEQE
//