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Database: UniProt
Entry: A0A0N0T8C6_9NOCA
LinkDB: A0A0N0T8C6_9NOCA
Original site: A0A0N0T8C6_9NOCA 
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
//
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