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Database: UniProt
Entry: A0A098M7Y4_9BACL
LinkDB: A0A098M7Y4_9BACL
Original site: A0A098M7Y4_9BACL 
ID   A0A098M7Y4_9BACL        Unreviewed;       667 AA.
AC   A0A098M7Y4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=PWYN_04370 {ECO:0000313|EMBL:KGE18689.1};
OS   Paenibacillus wynnii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=268407 {ECO:0000313|EMBL:KGE18689.1, ECO:0000313|Proteomes:UP000029734};
RN   [1] {ECO:0000313|EMBL:KGE18689.1, ECO:0000313|Proteomes:UP000029734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18334 {ECO:0000313|EMBL:KGE18689.1,
RC   ECO:0000313|Proteomes:UP000029734};
RA   den Bakker H.C.;
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGE18689.1, ECO:0000313|Proteomes:UP000029734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18334 {ECO:0000313|EMBL:KGE18689.1,
RC   ECO:0000313|Proteomes:UP000029734};
RA   Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (OCT-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGE18689.1}.
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DR   EMBL; JQCR01000002; KGE18689.1; -; Genomic_DNA.
DR   RefSeq; WP_036648847.1; NZ_JQCR01000002.1.
DR   AlphaFoldDB; A0A098M7Y4; -.
DR   STRING; 268407.PWYN_04370; -.
DR   eggNOG; COG1874; Bacteria.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000029734; Unassembled WGS sequence.
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:UP000029734}.
FT   DOMAIN          10..376
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          389..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;  75447 MW;  23178645777BD691 CRC64;
     MSKLRYGVAY YDEYMPYERL NEDIAMMKET GINVVRIAES TWSTHEPQNG VFDFSSVDRV
     LDAMHAAGIE VIVGTPTYAV PTWLVKEHPD VLAVTAKGPG RYGARQIMDI TNPVYLFHAE
     RIIRKLISRV CKHPAVIGYQ TDNETKHYDT AGDNVQLQFV KYMREKYDSL DIINSRFGLD
     YWSNRINSWE DFPSIVGTIN GSLGAEFARF QRGLVTNFLA WQVALVNEYK QPGQFVTQNF
     DFEWRGYSFG VQPSVDHFAA AEPFDIAGVD IYHPSQHELT GTEISFGGDM ARSLKRSNYL
     VLETQAQAFP QWTPYPGQLR LQAFSHLASG ADMVAYWHWH SIHNSFETYW KGLLSHDFKP
     NPVYNEAKTI GRDFQALSNQ LAGLRKDNKV AVMVSNEALT AMEWFKLPDG KTYNNVVRWM
     YDELYRMNIE CDFIQPSYKE LNQYSLIVVP ALYAAPDADL ERLNAYVKQG GHVVYSFKSG
     FTDEVVKVRT VEQPGIISEA CGIGYSLFVS PHEVPLKSAH ADIGAEDNHV ETWMELITST
     TAEVLLSYDH PAYGDYAAVT RNRYGLGTAT YIGCMTSSAM VGSVLKSTVK EAGLWSSDQE
     LSFPIIVKKG TNRAQQTVRY YFNYSNAAVS FTNIHVEGTE LLSGREVNKG EKLSLEPWGF
     LILLEKQ
//
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