ID A0A1Y4NP49_9FIRM Unreviewed; 681 AA.
AC A0A1Y4NP49;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=B5F07_15815 {ECO:0000313|EMBL:OUP81881.1};
OS Lachnoclostridium sp. An169.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965569 {ECO:0000313|EMBL:OUP81881.1, ECO:0000313|Proteomes:UP000195962};
RN [1] {ECO:0000313|Proteomes:UP000195962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An169 {ECO:0000313|Proteomes:UP000195962};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUP81881.1}.
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DR EMBL; NFKT01000025; OUP81881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4NP49; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000195962; 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: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:UP000195962};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 15..394
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 407..606
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 621..680
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 316
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 681 AA; 77666 MW; A2620A6CC8A1B42A CRC64;
MKIRKLPEKL LHGGDYNPDQ WLDCPEVLEE DIRLMKEAHV NCVSLGIFAW GKLEPEEGRY
ELDWLGGIID RLYDNGISTI LATPTGAMPH WLQENYEEVR QVLSNGIRKL PGGRHNFCPS
SPVMRKKMQG IDRALSKKFG KHPGVIAWHL SNEYAGGAGD NGDGACYCPL CQANFRKWLK
ERYHTLDNLN HAWWNSFWSN DITDWEQIHA PSTIGESTLD GLKLDWRRFV SDQILDFCKE
ERDVVREFSD RPVVTNLMGA FYPLDYFKWA KELDIVSLDN YPFWHYMEDE SLMASASSFA
HTLMRSLKKQ PYLLMESVPS AVQWGPKNTL KRPGMHALSS LQAIACGSDS VQYFQWRKGR
GGSEKYHGAV VDHKNGGNTR VFRDVADLGE RLEDIASRVL RTCNRPRAAI VFDWENRWAV
DGTAAVTNPF DYTHRWQRYY RAFWDLGMDV DIINMDDPLE GYSLIVAPYN YMYRGDYADR
VRKFTAGGGT YVTTCWSGEV DESSLCFTGK HPLSDVLGIR TEEIDVMPDY VHNRVICGDK
AYDIQDLCAL VHAEAAEVLG TYEKDFYAGY PAVTVNRYGE GKAYFIASAN EEPFYRDFLK
MVAEETGTGC TLKVSGELPK GVTVNERRGE EENDSLWFVQ NFNAGETAVV FEDTYRDIET
GEEVSGECVM KGYQCLILKK I
//
