ID D4G1N9_BACNB Unreviewed; 686 AA.
AC D4G1N9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 61.
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 Name=lacA {ECO:0000313|EMBL:BAI87020.1};
GN ORFNames=BSNT_09994 {ECO:0000313|EMBL:BAI87020.1};
OS Bacillus subtilis subsp. natto (strain BEST195).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=645657 {ECO:0000313|EMBL:BAI87020.1, ECO:0000313|Proteomes:UP000006805};
RN [1] {ECO:0000313|EMBL:BAI87020.1, ECO:0000313|Proteomes:UP000006805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEST195 {ECO:0000313|EMBL:BAI87020.1,
RC ECO:0000313|Proteomes:UP000006805};
RX PubMed=20398357; DOI=10.1186/1471-2164-11-243;
RA Nishito Y., Osana Y., Hachiya T., Popendorf K., Toyoda A., Fujiyama A.,
RA Itaya M., Sakakibara Y.;
RT "Whole genome assembly of a natto production strain Bacillus subtilis natto
RT from very short read data.";
RL BMC Genomics 11:243-243(2010).
RN [2] {ECO:0000313|EMBL:BAI87020.1, ECO:0000313|Proteomes:UP000006805}
RP GENOME REANNOTATION.
RC STRAIN=BEST195 {ECO:0000313|EMBL:BAI87020.1,
RC ECO:0000313|Proteomes:UP000006805};
RX PubMed=25329997; DOI=10.1371/journal.pone.0109999;
RA Kamada M., Hase S., Sato K., Toyoda A., Fujiyama A., Sakakibara Y.;
RT "Whole genome complete resequencing of Bacillus subtilis natto by combining
RT long reads with high-quality short reads.";
RL PLoS ONE 9:E109999-E109999(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP011541; BAI87020.1; -; Genomic_DNA.
DR AlphaFoldDB; D4G1N9; -.
DR SMR; D4G1N9; -.
DR STRING; 86029.AWV81_17965; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR KEGG; bso:BSNT_09994; -.
DR PATRIC; fig|645657.3.peg.241; -.
DR HOGENOM; CLU_012430_1_1_9; -.
DR Proteomes; UP000006805; 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|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 20..400
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 411..616
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 627..683
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 158
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 322
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 686 AA; 79180 MW; 5C7C8DFC1438F1B2 CRC64;
MSKLEKTHVT EAKFMLHGGD YNPDQWLDRP DILADDIKLM KLSHTNTFSV GIFAWSALEP
EEGVYQFEWL DDIFERIHSI GGRVILATPS GARPAWLSQT YPEVLRVNAS RVKQLHGGRH
NHCLTSKVYR EKTRHINRLL AERYGHHPAL LMWHISNEYG GDCHCDLCQH AFREWLKSKY
DNSLKTLNQA WWTPFWSHTF NDWSQIESPS PIGENGLHGL NLDWRRFVTD QTISFYKNEI
IPLKELTPDI PITTNFMADT PDLIPYQGLD YSKFAKHVDV ISWDAYPVWH NDWESTADLA
MKVGFINDLY RSLKQQPFLL MECTPSAVNW HNVNKAKRPG MNLLSSMQMI AHGSDSVLYF
QYRKSRGSSE KLHGAVVDHD NSPKNRVFQE VAKVGETLER LSEVVGTKRT AQTAILYDWE
NHWALEDAQG FAKATKRYPQ TLQQHYRTFW EHDIPVDVIT KEQDFSPYKL LIVPMLYLIS
EDTISRLKAF TADGGTLVMT YISGVVNEHD LTYTGGWHPD LQAIFGVEPL ETDTLYPKDR
NAVSYRSQIY EMKDYATVID VKTASVEAVY QEDFYARTPA VTSHEYQQGK AYFIGARLED
QFQRDFYEGL ITDLSLSPVF PVRHGKGVSV QARQDQDNDY IFIMNFTEEK QLVTFDQSVK
DIMTGDILSG DLTMEKYEVR IVVNTH
//
