ID A0A087AQ50_9BIFI Unreviewed; 691 AA.
AC A0A087AQ50;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN ORFNames=BIGA_1379 {ECO:0000313|EMBL:KFI60900.1};
OS Bifidobacterium pullorum subsp. gallinarum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=78344 {ECO:0000313|EMBL:KFI60900.1, ECO:0000313|Proteomes:UP000029046};
RN [1] {ECO:0000313|EMBL:KFI60900.1, ECO:0000313|Proteomes:UP000029046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11586 {ECO:0000313|EMBL:KFI60900.1,
RC ECO:0000313|Proteomes:UP000029046};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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 ECO:0000256|PIRNR:PIRNR001084};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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:KFI60900.1}.
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DR EMBL; JGYX01000003; KFI60900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087AQ50; -.
DR SMR; A0A087AQ50; -.
DR eggNOG; COG1874; Bacteria.
DR Proteomes; UP000029046; 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:0006012; P:galactose 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 Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013739; Beta_galactosidase_C.
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; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR PANTHER; PTHR36447:SF1; BETA-GALACTOSIDASE GANA; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08533; Glyco_hydro_42C; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR PIRSF; PIRSF001084; B-galactosidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:KFI60900.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:KFI60900.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029046}.
FT DOMAIN 27..399
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 414..614
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 635..691
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 322
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 691 AA; 77851 MW; 66114835FE491098 CRC64;
MMKNTHRAFR WPQPLEGQQA RIWYGGDYNP DQWPEEVWDE DIRLMTKAGV NVVSVAIFSW
AKIEPQEGVY DFDWLDRIID KLGKAGIAVD LASATASPPM WLTQKHPEVL WRDEYGHVCW
PGAREHWRPT SPVFREYALN LCRRMAEHYK DNPYVVAWHV SNEYGCHNRF DYSDDAMHAF
QRWCEERYGT IDAVNEAWGT AFWAQRMNDF SEIIPPRFIG EGNFMNPGKL LDFKRFSSDA
LKAFYIAERD LLAEITPGRP LTTNFMVSAP GTGLDYDDWG YEVDFVSNDH YFTPGEEHFD
ELAYSASLVD GIARKNPWWL MEHSTGAVNW RPINYRKEPG QLVRDSLAHL AMGADAICYF
QWRQSKAGAE KYHTAMLPHA GEDSQDFRDV CELGADLATL GNHGLTGTRL AKSRVAVVFD
YESQWATEHT ATPTQQVRHW TEPLAWFRAF ADNGVTADVV PIRGDWDSYE AAVLPSVYLL
DEANSQRVRD YVAKGGKLFA TYYTGISDER DHIWLGGYPG SIRDVVGVRI EEFAPMGGDF
PGALDHLDLD NGTVAHDFAD VITSTADTAT VLASFKSEPW VGMDGSPAIV ANSYGDGSTV
YVGCRLGREG LAASMPAMCE AIGFELPQSD GRVMRIERVS EDGADRFEFL FNRSHDRVSV
ETDGEPLVAS LGHVEDGRAV LDPNGVVIVR R
//
