ID A0A109Y5W2_ENTGA Unreviewed; 670 AA.
AC A0A109Y5W2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AL523_14870 {ECO:0000313|EMBL:AMG50947.1};
OS Enterococcus gallinarum.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1353 {ECO:0000313|EMBL:AMG50947.1, ECO:0000313|Proteomes:UP000055269};
RN [1] {ECO:0000313|Proteomes:UP000055269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_163 {ECO:0000313|Proteomes:UP000055269};
RA Case J., Tallon L., Sadzewicz L., Sengamalay N., Ott S., Godinez A.,
RA Nagaraj S., Nadendla S., Sichtig H.;
RT "FDA Database for Regulatory Grade Microbial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-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}.
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DR EMBL; CP014067; AMG50947.1; -; Genomic_DNA.
DR RefSeq; WP_016620424.1; NZ_CP014067.2.
DR AlphaFoldDB; A0A109Y5W2; -.
DR STRING; 1353.AL523_14870; -.
DR KEGG; ega:AL523_14870; -.
DR Proteomes; UP000055269; 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: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..383
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 394..600
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 305
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"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 670 AA; 76874 MW; 3AC3A77D6187CC73 CRC64;
MTKFFDRILF GGDYNPNQWP KEIWEEDIRI FKKASINSAT VNVFSWAKIQ PSENCYDFEE
LDQIIEKLST EGFDIVLATS TAALPAWMFK KYPEVARTDY DGRHHKFGQR HNACPNSLVY
QKYAERLATK LAERYGENPQ VTCWHINNEY GGECYCENCE KAFRVWLKDK YQTIEALNKA
WNMEFWGHTV YEWDEIVLPN ALSEGIGYDK TAFAGISIDY RRFNSDSLLK NYMMERDAIR
KIDPTTPITT NLMGTFKGLD YFKWAKEMDL ISWDNYPAYN TPWSLVAMTH DLMRGLKQQP
FMLMEQTPSQ QNWQPYNSLK KPGQMRAQSY QTIAHGADTI QYFQLRRSIG ACEKFHGAVI
EHVGHEDTRV FRETAALGAE LAQLSDIIGT QTQAQVAVIF DWDNYWALEY TSGPTVDLKY
VEQIHRYYRY FHEQNIAVDL VPVDADLSKY KLVAAPVLYM IKEGMQERLT DFVKQGGSLL
TTYMSGIVDQ SDNVHLGGYP GPLRELAGIW VEEIDALAPE QSNGVSLVNE ELTGTSNLVS
DLIHLETAEA LAHYTSNFYA GMPAVTKNMF GDGTVYYFGG QLEDQLQDQL FKTIVEENDI
TPVIEEATKL EVACRENAEA KFFVIINFHE EAQPLPAMFV GKTDLLTGEV LSSEMMLTQY
TTYIVKEERN
//
