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Database: UniProt
Entry: A0A1D9NX51_9FIRM
LinkDB: A0A1D9NX51_9FIRM
Original site: A0A1D9NX51_9FIRM 
ID   A0A1D9NX51_9FIRM        Unreviewed;       673 AA.
AC   A0A1D9NX51;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=bhn_III010 {ECO:0000313|EMBL:AOZ94958.1};
OS   Butyrivibrio hungatei.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=185008 {ECO:0000313|EMBL:AOZ94958.1, ECO:0000313|Proteomes:UP000179284};
RN   [1] {ECO:0000313|Proteomes:UP000179284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB2003 {ECO:0000313|Proteomes:UP000179284};
RA   Palevich N., Kelly W.J., Leahy S.C., Altermann E., Rakonjac J.,
RA   Attwood G.T.;
RT   "The complete genome sequence of the rumen bacterium Butyrivibrio hungatei
RT   MB2003.";
RL   Submitted (OCT-2016) 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; CP017830; AOZ94958.1; -; Genomic_DNA.
DR   RefSeq; WP_071174790.1; NZ_CP017830.1.
DR   AlphaFoldDB; A0A1D9NX51; -.
DR   KEGG; bhu:bhn_III010; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000179284; Chromosome ii.
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: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:SF1; BETA-GALACTOSIDASE GANA; 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   Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179284};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT   DOMAIN          15..388
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          400..604
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          613..660
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        151
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         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         161
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   673 AA;  77722 MW;  A0D8196E2BFCEEB3 CRC64;
     MVESSKVQKI LYGGDYNPEQ WPEDIWEEDM RLFKEAHIDI VTLNVFSWAQ LQPSEDTYDF
     SKLDKIMELV QKNGLKVCMA TSTAAHPAWM ARKYPDILRT EKNGVKRKFG SRHNSCPNSP
     TYRKYASKLV EKLAERYKDY DNIVCWHISN EFGGECYCEN CEKRFRSWVK DKYKTIEEVN
     RAWNMAFWGH TLYDFEDIVT PDLRSEEFEW DGIRTNFQGI SLDYARFNSD SLLECFLLEK
     EILKKYTPDI PVTTNLMGMY KPLDYQKWAE YMDFVSWDNY PTYNAKPYEP ALSHDLMRGC
     KNGKPFALME QTPGVTNWHL YCSLKRPGVM RLYSYQAMAH GADTVMFFQM RRSIGACEKY
     HSAVIDHVGT SDTRVFREVS ALGKELETIG SSILGARSKA EIAIVFDWDN WRAIDWSAGP
     SRLLNYCDQI KKYYYALWRN HYPVDIISVK DDLSKYKLVI APMLYMCKKG YDQTIRSFVE
     NGGTFVTTTF SGYVDDNDLV VTGGYPGKLK DILGIWVEEL DALPPEEANS FIYKGTEYPA
     QVLCDVLHLR SANELAKYEK DFYAGAPVIT VNAFGAGKAY YFATQSNDDF YKEFLSDICS
     ECGVQPLLKC DEDLEVTERS NSNGDFLFVL NHSQEKKEFV LPYDACNLVT GTEYFKGKEI
     KISGKDAMIL IKK
//
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