ID L1P463_9FLAO Unreviewed; 667 AA.
AC L1P463;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=HMPREF9078_00152 {ECO:0000313|EMBL:EKY10242.1};
OS Capnocytophaga sp. oral taxon 380 str. F0488.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1127693 {ECO:0000313|EMBL:EKY10242.1, ECO:0000313|Proteomes:UP000010436};
RN [1] {ECO:0000313|EMBL:EKY10242.1, ECO:0000313|Proteomes:UP000010436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0488 {ECO:0000313|EMBL:EKY10242.1,
RC ECO:0000313|Proteomes:UP000010436};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKY10242.1}.
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DR EMBL; AMES01000010; EKY10242.1; -; Genomic_DNA.
DR AlphaFoldDB; L1P463; -.
DR PATRIC; fig|1127693.3.peg.147; -.
DR HOGENOM; CLU_409748_0_0_10; -.
DR Proteomes; UP000010436; 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;
FT DOMAIN 191..365
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 378..546
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
SQ SEQUENCE 667 AA; 75420 MW; 40F2853C1169BF88 CRC64;
MFLRSYIWLL LLGIASITTT VKAQPYVSPI VAQVFIEPGQ TDEEINTWFK LLSEHQMNCC
RIRMFENYMK RPDGTWDFSL FDKAFKAAER YNVKIVGTLF PAAPDNSLGG FKHPYSQSHL
QEIATYIKQV VTHFKTSPAL YGWVLMNEPG TGGWVPNDAF ANTQKSEWLK TLQPTTYNSK
GYPQIVDFAP QQFLLHYNTW YLQWIANEVK KYDPNAYLHV NSHQIFSNIA EYNFPAWRNF
LSSLGASAHP SWHYTMLHRN QYATALGANC AIIRSGAGEL PFWVTELQGG NNTYSGYKAF
CPTKEEITQW LWTSIGNGAE HILFWCLNPR AVGDEAGEWA LVDFQNQPTD RLTAASEVAK
TLRKINISKF KPVVANIHIL YTRETLWVEK KAQLNDNANN DYEGRNTGGA MKSAFAMYET
LLENGINSQF QCFDEFNWNK PSYKGETIIL SGQISLPSRY WEPLHNFVRN GGKLIMEGLS
AFYDENMFAL HHTGFPLQDV LGGALKEVKC LPTDFSVNYQ NAPLPTHLWK GSIYNTQGQI
VAQEGNSVLA TRHRFVRGET FWFPSLLGLG ALRSGKGEAL SHLLLAEVQA AVPFQFETYQ
KGVQMYTMQK GNQYLTILIN KRPQATTVAL RCPKGVNPSV VFADKGGSAT ANTARLSSEE
TLVILWK
//
