ID L1Q3V2_9FLAO Unreviewed; 688 AA.
AC L1Q3V2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=HMPREF9073_00139 {ECO:0000313|EMBL:EKY22581.1};
OS Capnocytophaga sp. oral taxon 326 str. F0382.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1035193 {ECO:0000313|EMBL:EKY22581.1, ECO:0000313|Proteomes:UP000010441};
RN [1] {ECO:0000313|EMBL:EKY22581.1, ECO:0000313|Proteomes:UP000010441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0382 {ECO:0000313|EMBL:EKY22581.1,
RC ECO:0000313|Proteomes:UP000010441};
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:EKY22581.1}.
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DR EMBL; AMEU01000015; EKY22581.1; -; Genomic_DNA.
DR AlphaFoldDB; L1Q3V2; -.
DR STRING; 1035193.HMPREF9073_00139; -.
DR PATRIC; fig|1035193.3.peg.129; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_409748_0_0_10; -.
DR OrthoDB; 9774262at2; -.
DR Proteomes; UP000010441; 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 212..385
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 399..565
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
SQ SEQUENCE 688 AA; 78131 MW; A0671C141AA556DA CRC64;
MDKDFIALPL QHKMYHQKSI CMFLRSYIWL LLLGIASITT TVKAQPYVSP IGAQVFIEPG
QSDEEINTWF KLLSEHQMNC CRIRMFENYM KRPDGTWDFS LFDKAFKAAE RYNVKIVGTL
FPAAPDNSLG GFKHPYSQSH LQEIATYIKQ VVTHFKTSPA LYGWVLMNEP GTGGWVPNDA
FANIQKSEWL KTLQPTAYNS KGYPQIVDFT PQQFLLHYNT WYLQWIANEV KKYDPNAYLH
VNSHQIFSNI AEYNFPAWRN FLNSLGASAH PSWHYTMFHR NQYATALGAN CAIIRSGAGE
LPFWVTELQG GNNTYSGYKA FCPTKEEITQ WLWTSIGNGA EHILFWCLNP RTVGDEAGEW
ALVDFQNQPT DRLIAASEVA KTLRKINISK FKPVVANIHI LYTRETLWVE KKAQLNDNTN
NDYEGRNTGG AMKSAFAMYE TLLENGINSQ FQCFDEFNWN KPSYKGETII LSGQISLPSR
YWEPLRNFVR NGGKLIMEGL SAFYDENMFA LHHTGFPLQD VLGGALKEVK CLPTDFSVNY
QNAPLPTHLW KGSIYNTQGQ IVAQEGNSVL AMRHRFVRGE TFWFPSLLGL GALRSGKGEA
LSHLLLAEAQ PTVPFQFETY QKGVQMYTMQ KGNQYLTILI NKRPQATSVA LRCPKGVNPS
VVFADKGGST TANTARLSSE ETLVILWK
//
