ID A0A139B5Y4_9BIFI Unreviewed; 708 AA.
AC A0A139B5Y4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=BPS1E_0780 {ECO:0000313|EMBL:PAC73691.1};
OS Bifidobacterium pseudocatenulatum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=28026 {ECO:0000313|EMBL:PAC73691.1, ECO:0000313|Proteomes:UP000216789};
RN [1] {ECO:0000313|EMBL:PAC73691.1, ECO:0000313|Proteomes:UP000216789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1E {ECO:0000313|EMBL:PAC73691.1,
RC ECO:0000313|Proteomes:UP000216789};
RX PubMed=28837128; DOI=10.1038/ismej.2017.138;
RA Milani C., Mangifesta M., Mancabelli L., Lugli G.A., James K., Duranti S.,
RA Turroni F., Ferrario C., Ossiprandi M.C., van Sinderen D., Ventura M.;
RT "Unveiling bifidobacterial biogeography across the mammalian branch of the
RT tree of life.";
RL ISME J. 11:2834-2847(2017).
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:PAC73691.1}.
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DR EMBL; MNLB01000003; PAC73691.1; -; Genomic_DNA.
DR RefSeq; WP_065438839.1; NZ_RCXS01000001.1.
DR Proteomes; UP000216789; 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 26..384
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 401..616
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
SQ SEQUENCE 708 AA; 78982 MW; A55CEF0F1161EBD7 CRC64;
MSRYEADHIL FGAAYYDEYL MMKGIDRVDE DMRMMKEAGL NVIRIAESTW STCEPQPGVF
DFTYVDRALD AAQRAGIDVI VGTPTYAVPS WLVKLDPSVL AVTPNGEGKY GARQIMDIVN
ATYRFYGERV IRKLISHVAD HPAVIGYQVD NETKYYDSVS NDMQRLFIKY LYEKFDGDLN
ELNHRFGLDY WSNRINSWED FPDVTATINE SLGGEFDKFR RDQVRAFLQW QSDIVREYAH
DDQFITHNFD FEWRGYSFGV QPAVDHFKAA TAVDITGVDI YHPTEDDLTG KEIAFGGDMT
RSTKDGKNFL VLETEAQGQH GWVPFPGQLR LQAYSHLASG ADMVEYWHWH SIHNSFETYW
KGLLSHDLEP NPTYREAGVF GHEIGKPEVG ERLVHLKKQN KVAIMVSNES LTALDWFLIE
AGFPFGGNLK YNDVVRNVYD ALFELNVECD FVPSDAPAER LAKYEMIVTP ALYCTSQETT
DRLRTFVENG GHLVSTMRSF VSDDEVTVWA DRAPHNLTDV FGMTYSQFTR PNGHVSVEFA
GALAETASTD AQSLIELLNA DADTEVLASY GHYAWKDYAA VTRHAFGKGD AEWIATLLDA
DSIRAVMREA VEHAGVAVAG TALAGQISVR QGVNALGENV TYLLNYSADE VTVASPVAGE
VVVAPVVIAT DGNIDEAATA EVVLKEGTAV KEGDPLAIGR WNVVVIAG
//
