ID N4WBI7_9BACI Unreviewed; 681 AA.
AC N4WBI7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=J416_09856 {ECO:0000313|EMBL:ENH96599.1};
OS Gracilibacillus halophilus YIM-C55.5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=1308866 {ECO:0000313|EMBL:ENH96599.1, ECO:0000313|Proteomes:UP000012283};
RN [1] {ECO:0000313|EMBL:ENH96599.1, ECO:0000313|Proteomes:UP000012283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM-C55.5 {ECO:0000313|EMBL:ENH96599.1,
RC ECO:0000313|Proteomes:UP000012283};
RA Sugumar T., Polireddy D.R., Antony A., Madhava Y.R., Sivakumar N.;
RT "Draft genome sequence of Gracibacillus halophilus YIM-C55.5, a moderately
RT halophilic and thermophilic organism from the Xiaochaidamu salt lake.";
RL Submitted (MAR-2013) 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:ENH96599.1}.
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DR EMBL; APML01000036; ENH96599.1; -; Genomic_DNA.
DR RefSeq; WP_003469369.1; NZ_APML01000036.1.
DR AlphaFoldDB; N4WBI7; -.
DR STRING; 1308866.J416_09856; -.
DR PATRIC; fig|1308866.3.peg.1999; -.
DR eggNOG; COG1874; Bacteria.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000012283; 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: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:SF2; BETA-GALACTOSIDASE YESZ; 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 Reference proteome {ECO:0000313|Proteomes:UP000012283};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 16..394
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 405..611
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 624..679
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 152
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 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 681 AA; 79103 MW; 863852D906408655 CRC64;
MIHDVLNEKE ITLGVCYYPE HWPKDLWESD FQRMKELGFT YVRMGEFAWT IFEPEEGIYD
FTLFDEAIEV AKKYDLKVIM GTPTATPPVW VTEKYPEVLN VSQSGVQFKH GARRHYNYNS
EKYQELSANI VNQMAAHFKD HPTVVGWQID NELNCEINVF YSDADHHQFR QWVKRKYQTL
DQLNDAWGTV FWNQTYTSWE QVYLTQPTVN DSHNPHQALD EKRFFSDSAI AFAKLQADVI
RSHTNTQWIT TNGMFKHLDN HQLTQNVLDF YAYDSYPNFN KIIPDDSKKP LQDRKWSFNL
SNVRSFGGNF AIFEQQAGPG GWVNRIEQPT PKPGQLRLWT YQSIAHGADQ ILYFRWRTAT
KGSEIYWHGI NDYHNQRNRR IDEIDQVSHE IKKIGSSLVG SSYQAKAAIV IDYQNEWDGE
VDRWYGDFID QSQEAWFKAF QYQHIPVDLL NIEQAKTVED LNGYQVLIYP HAAILTKETA
NLFSEYVKQG GTAIFGCRTG YKDLTGQTYM MKHPGYLADL TGSTVEEYTL ISPLQERPTV
SLFHGDPVTT EGFNEVLSLE DSDVEMIGSF DNAYYRGKPA ATKRKFGQGY AYYFGGVFSY
DIAEQMLQDL HIQRSDALSL PEKVEIAIRV KENRTFYILL NFASSDQLIT IHQKMVNIVK
EQVLRGDYIM KAYDVLVLES Q
//
