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Database: UniProt
Entry: A0A2T0TLQ0_9PSEU
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ID   A0A2T0TLQ0_9PSEU        Unreviewed;       665 AA.
AC   A0A2T0TLQ0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=CLV43_101852 {ECO:0000313|EMBL:PRY46575.1};
OS   Umezawaea tangerina.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Umezawaea.
OX   NCBI_TaxID=84725 {ECO:0000313|EMBL:PRY46575.1, ECO:0000313|Proteomes:UP000239494};
RN   [1] {ECO:0000313|EMBL:PRY46575.1, ECO:0000313|Proteomes:UP000239494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44720 {ECO:0000313|EMBL:PRY46575.1,
RC   ECO:0000313|Proteomes:UP000239494};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-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   -!- 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:PRY46575.1}.
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DR   EMBL; PVTF01000001; PRY46575.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0TLQ0; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000239494; 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   Reference proteome {ECO:0000313|Proteomes:UP000239494};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT   DOMAIN          16..387
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          398..599
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   ACT_SITE        152
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        310
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         162
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         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   665 AA;  73513 MW;  F8374516B0B7B26F CRC64;
     MTSWPSGVRG LAWGADYNPE QWPEHVWAED VELMRRAGVN LVSVGIFSWA LLERADGEYD
     FGWLDRALDL LHEGGIRVDL ATATASPPPW LTTAHPEMLP QRADGTRYSH GSRQEYCPSS
     PVYRAKAVAL ATALAERYRD HPALAAWHVG NEYGCHVARC YCDRCAEAFR EWLRRRHGDL
     DALNEAWATA FWSQHYTAWD QILPPRLTPT FGNPGHLLDF DRFCSDALLE LYKAERDVLH
     ATTPGVPVTT NFMVGWTFDA LDYWAWAAEV DFVSNDHYTR SESAERHVEL AMAADLTRGL
     AGGRPWLLME HSTSAVNWQP RNIAKLPGEM RRHSFAHTAR GADGTLFFQW RQSRAGAERY
     HSAMVPHAGV ETKVYREVCE VGAEYAKLTE LLGSTVDASV AIVYDWQSRW LSGQEAHPTQ
     DFSYQDTVFA LYRQLWAAGV TVDFVPPSGD LSPYRLAVVP ALYSVTDADA ARLAEYVDGG
     GHVLVTYMSG LTDERGHVRL GGYPGAFRDL LGVWTEEFFP LREDEVVRLD DGGVAAVWTE
     LLHTRGAEVV SAYADGPLPG VPAVTRNRHG AGTAWYLACG LGDDGLRRLV DAALEDAGVP
     ARPGLEIVRR RGTRDGDAVS WLVAVNHEAH DVALPATGVE LLSGSRVDSS LVVPAGAVVV
     LREEV
//
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