ID A0A3G3JT07_9BACL Unreviewed; 687 AA.
AC A0A3G3JT07;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=EAV92_01235 {ECO:0000313|EMBL:AYQ71332.1};
OS Cohnella candidum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=2674991 {ECO:0000313|EMBL:AYQ71332.1, ECO:0000313|Proteomes:UP000269097};
RN [1] {ECO:0000313|EMBL:AYQ71332.1, ECO:0000313|Proteomes:UP000269097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=18JY8-7 {ECO:0000313|EMBL:AYQ71332.1,
RC ECO:0000313|Proteomes:UP000269097};
RA Srinivasan S., Kim M.K.;
RT "Genome Sequence of Cohnella sp.";
RL Submitted (OCT-2018) 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 ---------------------------------------------------------------------------
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; CP033433; AYQ71332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G3JT07; -.
DR KEGG; coh:EAV92_01235; -.
DR Proteomes; UP000269097; 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 Reference proteome {ECO:0000313|Proteomes:UP000269097};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 20..391
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 403..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 314
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 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 687 AA; 77689 MW; F2AC4F8D429C2860 CRC64;
MSNKFPPISA KLPVFMHGAD YNPDQWLHDP AVLEEDIRLM KLAHCNVMAV GIFSWATLEP
EEGTFRFDWL DNVLDQFAEN GIYAWVATPS GARPAWMSQK YPEVLRVAPN RQRNLHGLRH
NHCYTSPVYR EKVTIMNREL ARRYSQHPAV VGWHISNEFG GECHCDYCQE AFRAWLMRKY
GSLEALNAAW WTAFWSHTYT DWSQVESPAP HGETMVHGQN LDWRRFVTDQ TIDFYKHEIV
PLKEANPELP CTANMMDLFE GLDYRKFAEA VDVISWDAYP TWHASDLEAA VGSWFAFNHD
LFRSLKRKPF MLMESTPSLT NWQPVSKLKR PGMHRLSSLQ AVAHGSDTVQ YFQWRKSRGS
SEKFHGAVVD HVGHEHTRVF KDVASLGETL SGLTELIGTP VPAEAAVLFD WDNRWAVKDA
QGPRNQGIHY EETVMQHYRA MWELGIPTDV VGSGDDFGAY KLIAVPMAYL LREETGKRLE
KFVENGGTLL ATYWTGIVDE NDLCHLGGFP GPLRKTLGIW AEEIEGLHDH DRNGLEMNAG
NALGIEGTYE VRELCDLIHA EGASVLGVYE SDFYAGRPAL TMNAFGRGQA YYLAARVSDP
AFYEKLYGRL AADAGVRRAL NSALPAGVTA QLRSDGERDY VFVMNFSGTE AEVVLDRVYE
DAETGEETSG VMRLPVHGIR LLKRSAL
//
