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Database: UniProt/TrEMBL
Entry: I0BSU2_9BACL
LinkDB: I0BSU2_9BACL
Original site: I0BSU2_9BACL 
ID   I0BSU2_9BACL            Unreviewed;       691 AA.
AC   I0BSU2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=B2K_32840 {ECO:0000313|EMBL:AFH65439.1};
OS   Paenibacillus mucilaginosus K02.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH65439.1, ECO:0000313|Proteomes:UP000007392};
RN   [1] {ECO:0000313|EMBL:AFH65439.1, ECO:0000313|Proteomes:UP000007392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K02 {ECO:0000313|EMBL:AFH65439.1,
RC   ECO:0000313|Proteomes:UP000007392};
RA   Xiao B., Sun L., Xiao L., Lian B.;
RT   "Complete genome sequence of Paenibacillus mucilaginosus K02.";
RL   Submitted (JUN-2013) 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; CP003422; AFH65439.1; -; Genomic_DNA.
DR   RefSeq; WP_014652721.1; NC_017672.3.
DR   AlphaFoldDB; I0BSU2; -.
DR   KEGG; pmw:B2K_32840; -.
DR   PATRIC; fig|997761.3.peg.6597; -.
DR   HOGENOM; CLU_012430_1_1_9; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000007392; 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   Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT   DOMAIN          14..386
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          398..607
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          616..672
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        150
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         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   691 AA;  77944 MW;  2E580F5159B373D9 CRC64;
     MINKKLPKMF YGGDYNPEQW DKPVWDEDMR MFQLAGIDVA TVNVFSWALL QPSENEYNFE
     LLDEIMDKLH ENGLYACLAT STGAHPAWMA HRHPDVLRVD FQGRKRKFGG RHNSCPNSPT
     YRKYARLLAG KLAERYKDHP ALLVWHVSNE YGGECYCDNC AAAFRVWLQQ RYGSLEAVNK
     AWNTRFWGHT FYDWEEIVPP NELSEQWGPT RTNFQGISLD YTRFNSDSLL ECYKEEHEEL
     KKHTPDIMVT TNLMGTFKPL DYFKWAKHMD IVSWDNYPAA DTPVSRTAMT HDLMRGLKDG
     APFMLMEQTP SQQNWQPYNS LKRPGVMRLW SYQAVARGAD TVMFFQLRRS VGACEKYHGA
     VIEHVGHEHT RVFRECAQLG AELQQLGDSL LDSRVPSRAA IVFDWENWWA VEFSSGPTVA
     LQYVEEVHKY YDALYQANIQ VDMIGTDADL SGYDVVIAPV LYMVKSGYAK KVEEFVQGGG
     TFLTTFFSGI VNENDIVTLG GYPGELRKVL GIWAEEIDAL LPGKQNRIVM KKELGSLQGE
     YACEMLCDLI HSEGAEIIAE YGDDFYQGMP VVTANTFGQG QAWYLASSPE PSFLQGLLQQ
     LCRDKGIEPL LETPAGVEVS RRRKDGKDYY FLLNHNAAPQ TVDAAALDAV DVLAGGKAGI
     VELPAHGAVI LQAAASAEDT RSGSAQGVLS R
//
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