ID M5P5D9_9BACI Unreviewed; 666 AA.
AC M5P5D9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=BSONL12_12706 {ECO:0000313|EMBL:EME74649.1};
OS Bacillus sonorensis L12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1274524 {ECO:0000313|EMBL:EME74649.1, ECO:0000313|Proteomes:UP000011907};
RN [1] {ECO:0000313|EMBL:EME74649.1, ECO:0000313|Proteomes:UP000011907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12 {ECO:0000313|EMBL:EME74649.1,
RC ECO:0000313|Proteomes:UP000011907};
RX PubMed=23538904;
RA Adimpong D.B., Sorensen K.I., Nielsen D.S., Thorsen L., Rasmussen T.B.,
RA Derkx P.M., Jespersen L.;
RT "Draft Whole-Genome Sequence of Bacillus sonorensis Strain L12, a Source of
RT Nonribosomal Lipopeptides.";
RL Genome Announc. 1:E0009713-E0009713(2013).
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:EME74649.1}.
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DR EMBL; AOFM01000007; EME74649.1; -; Genomic_DNA.
DR RefSeq; WP_006638525.1; NZ_AOFM01000007.1.
DR AlphaFoldDB; M5P5D9; -.
DR STRING; 1274524.BSONL12_12706; -.
DR GeneID; 79846105; -.
DR PATRIC; fig|1274524.3.peg.2741; -.
DR eggNOG; COG1874; Bacteria.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000011907; 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: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 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; 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; 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|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 11..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 DOMAIN 603..657
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 146
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"
SQ SEQUENCE 666 AA; 74943 MW; BF9A5A192D44CBC2 CRC64;
MKQQKLYHGA CFYPELWNEA VLEEDIHMMK ETGINVVRIG EFAWSKMEPE EGCFDISFFA
HVIRKLAANE IETVMCTPTA TPPIWLTHGH PERIHVNEKG ETMGHGSRQH VCTNHPYFRE
RARLITEHIA KEIGGLPGLA GWQLDNELKC HVSECMCETC KTLWHKWLKE RYQSIDRLNE
AWGTGVWSVT YQTFEQIPQP GPTPFLHHSS LKTMYQLFSM EKITEFAHEQ AAVIRKHSDA
PITHNSSIMF GVNNEDLFSG LDFASFDTYA SQENRAAFLF NCDLWRNMKK GRAFWIMETS
PSYSASLESY ALPHEDGYLR AEAVSSYALG SEAFCYWLWR QHRAGSEQPH GSILSAWGEQ
DVGYRNVLEV ERARKEIEDA VLSTVPVQAE TAVVYSDRAK AFLKTEPHRQ LHYRSLITDF
YDRFLSLGIH RDVILEGSTL AGYKLLFTPF IHYLPPEFIK KASAFTENGG IWIAGPLTGG
RTEHHTIHTD CGLGPLETYA GVKTLFTFPL DERRTVGSAF GIKAPLSLWS AVFEADPAEA
VGIIEQGPAS GKAFMTEHKR GKGKIVMLGS MPAGEAGDMM LKKMISHYAE EAGVTLNMNV
TPGTIVAPRM GPDGTLWVIV NMDGKGGEVV LPYNAADVIT NNREARGRLK LGPYQYRTLL
FPAARQ
//
