ID A0A0N0T8C6_9NOCA Unreviewed; 659 AA.
AC A0A0N0T8C6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=ADL03_22120 {ECO:0000313|EMBL:KOV82936.1};
OS Nocardia sp. NRRL S-836.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV82936.1, ECO:0000313|Proteomes:UP000037746};
RN [1] {ECO:0000313|Proteomes:UP000037746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-836 {ECO:0000313|Proteomes:UP000037746};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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:KOV82936.1}.
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DR EMBL; LGDY01000103; KOV82936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0T8C6; -.
DR STRING; 1519492.ADL03_22120; -.
DR PATRIC; fig|1519492.3.peg.4750; -.
DR Proteomes; UP000037746; 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: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 Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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; 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; 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 13..379
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 390..590
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT ACT_SITE 149
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 302
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
SQ SEQUENCE 659 AA; 71842 MW; 70ECEFC108F7897F CRC64;
MTDRLGGLAF GGDHNPEQWD EQVWEEDDEL MRVAGVNLAT VGVFSWALLE PEEGRYDFGW
LDAHLDRLHA NGVAVDLATP TASPPPWFTL AHPDALPVTA EGARLVHGSR DTYCLTAPAY
RAAARRIAAA LAERYGDHPA LALWHVHNEY ATLCYCEHTA AAFRMWLRDR YGTLDALNES
WGTAFWSQRY GSWEQVLPPR ATQWHRNPGH TLDFSRFFSD EVVAAYREQR DAIRAHSDRP
VTTNLMMPGY QNVDLWKLGR EVDVVAIDHY PDRPGRSAAA DAAFAADRAR SFAGGRPWLL
MEQGTSTVYD RGRTLAKEPG EILRHSLAHI ARGSEGALFF QWRQSKAGAE QWHSAMVPHA
GPDSRVFREV AATGAAVARL AALAGSVVTA EVAVLHDSDA WWGLSSDGLP SSELDYHSAL
RNAHRAVWDA GVVADFAHPE ADLGRYRLVL APALYLLSDA GAENLRRYVA DGGTVLVQHF
SGVVDDRAQA RLGGYPAAPL REALGIRVEE YRPLRHGERI TLSDGSHGTV WSESVRPQGA
ETVAAYTDGM LAGSPAITRH DFGAGHGWYL STRLDDADYT ALVARLLDTV GVGPVLPGLP
PGTEAVTRVA ADGRRWHFVL NHRTEPVQLP TPAHDLLTDG PVAGLPPGGC AVLNGGTSL
//