ID V2Y260_9FIRM Unreviewed; 671 AA.
AC V2Y260;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=GCWU0000282_003088 {ECO:0000313|EMBL:ESL01791.1};
OS Catonella morbi ATCC 51271.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Catonella.
OX NCBI_TaxID=592026 {ECO:0000313|EMBL:ESL01791.1, ECO:0000313|Proteomes:UP000018227};
RN [1] {ECO:0000313|EMBL:ESL01791.1, ECO:0000313|Proteomes:UP000018227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51271 {ECO:0000313|EMBL:ESL01791.1,
RC ECO:0000313|Proteomes:UP000018227};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUN-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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940}.
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:ESL01791.1}.
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DR EMBL; ACIL03000020; ESL01791.1; -; Genomic_DNA.
DR RefSeq; WP_023355930.1; NZ_KI535370.1.
DR AlphaFoldDB; V2Y260; -.
DR STRING; 592026.GCWU0000282_003088; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_2_0_9; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000018227; 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:UP000018227}.
FT DOMAIN 11..387
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 399..592
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
SQ SEQUENCE 671 AA; 77560 MW; D55A2B82981E27B3 CRC64;
MENEFLYGCA YYPEYMPYER IDEDFALMQK AGMNVVRIAE STWSTLEPRE GQYNFYYIDE
VLKRAGQYGL KVIIGTPTYA IPSWLARLDE NVLVHTKNGD MKYGKRRIFN LLSDTYIFYG
SRIIRKLLEH TVNHPQVIGF QIDNETKHYD NYGAEIQEGF VNFLKSRYSD IEEFNRDYGL
AYWSNSIHSW EDFTDISGTI NASLSCEFEE FQRETAVNFL KMQAEIINEY KNPNQFITHN
FDFEWHKFGA DIAQDGYSYG VQDGINHFNA AKSLTHAGTD IYHPTGFKLT GAEIAFCGDE
IRNLKNDNYF VLECQSQAFK YWCPFPKQLR LHAFSHIASG ADGILYWNWH SIHQSYETYW
KGILSHDLKP GRIYDEISQI GNEIKTLTKE KLCIKKNNKI ALLVDTLSLS AFKWFPIDKN
LSYNDVVRYI YDSLYEKNFE CDVVFSECAD ISKYEAIVCP ALYCVSEALL KRLDDFVKNG
GILIGGFRSF VADRKVSVYK ETLPAGLTEC FGIHYDEFTH TLNMKVGGRE VKYVAELITI
DSATELYPYE HRYWDRYSAI TCNEYGRGKA YYIGAYPDKE VLKKVLNQAL AEIRKKQNVP
ISAGFPIITR SGVNEAGEEL TYVFNYSLSD ADIFIDGDNE TGYKDIISGK SYVKGDKIKL
EDWDLVVLKK M
//
