ID A0A1I2SET9_9FIRM Unreviewed; 668 AA.
AC A0A1I2SET9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=SAMN04487761_12330 {ECO:0000313|EMBL:SFG51324.1};
OS Lachnospiraceae bacterium C7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1792306 {ECO:0000313|EMBL:SFG51324.1, ECO:0000313|Proteomes:UP000198643};
RN [1] {ECO:0000313|EMBL:SFG51324.1, ECO:0000313|Proteomes:UP000198643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 {ECO:0000313|EMBL:SFG51324.1,
RC ECO:0000313|Proteomes:UP000198643};
RA de Groot N.N.;
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940}.
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DR EMBL; FOPE01000023; SFG51324.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2SET9; -.
DR STRING; 1792306.SAMN04487761_12330; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000198643; 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: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 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; 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; PF08532; Glyco_hydro_42M; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000198643}.
FT DOMAIN 12..378
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 426..588
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
SQ SEQUENCE 668 AA; 77416 MW; 0C24018050450A49 CRC64;
MKTEKILFGV AYYDEYIPYD RIDKDMKMMK EAGINVIRIA ESTWSTWEPQ EGVFNFTHLH
RMLDTSNKYG ISVIIGTPTY AIPSWLAKKD DSILTTTHNG KNLYGPRQNM DITNKTYLKY
AKRIIIKLLD EVKDAPNVIG YQIDNETKAY DTCSSSAQKL FINYLKEKYL NINEFNQEFG
LNYWSNRIEN WEDFPDIRGT INGSLDAEYK KFQRNLVTKF LAWQADIINK YKKENQFLTQ
NFDFGWHDYS FGLQPEVDHF QSSKCIDVTG CDIYHPAQSK LTGCEITACG NIARGTKRSN
YLVLETEAQG NPQWLPYPNQ LKLMAFSHIA NGSNSVMYWH WHSIHNAIES YWKGVLSHDF
SKNVTYKEIS SIGNKFAQIG DKLKNLKKKN KIAIVADNAS LTGLSEFPTE TLKERSYNTF
FRWVCDALYK LNFEYDVINT EPSLLYDYNL VIIPTLYCAT EKYLNAINEY VKCGGNVIVT
FKSGFSNEHL KIYHDTQPHI INEALGVKYD QFTYSDNVTI EYNSKVSETK EWLELVRCTT
AKTLAYYNHK YWNEYSAISR NDYGTGHSLY LATYFSSEML IDVISDFIDY IDFKDDISKL
PTQCQYPIVV KQGINDYGKN IVYYLNYNDS TMQVKNIAGN GINLITTNSI KQNETFTLEP
WGFAVVEY
//