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Database: UniProt
Entry: A0A087ASQ3_9BIFI
LinkDB: A0A087ASQ3_9BIFI
Original site: A0A087ASQ3_9BIFI 
ID   A0A087ASQ3_9BIFI        Unreviewed;       695 AA.
AC   A0A087ASQ3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
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_0327 {ECO:0000313|EMBL:KFI61803.1};
OS   Bifidobacterium pullorum subsp. gallinarum.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=78344 {ECO:0000313|EMBL:KFI61803.1, ECO:0000313|Proteomes:UP000029046};
RN   [1] {ECO:0000313|EMBL:KFI61803.1, ECO:0000313|Proteomes:UP000029046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 11586 {ECO:0000313|EMBL:KFI61803.1,
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:KFI61803.1}.
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DR   EMBL; JGYX01000001; KFI61803.1; -; Genomic_DNA.
DR   RefSeq; WP_033507957.1; NZ_JGYX01000001.1.
DR   AlphaFoldDB; A0A087ASQ3; -.
DR   eggNOG; COG1874; Bacteria.
DR   OrthoDB; 9800974at2; -.
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: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   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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; 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; 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:KFI61803.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:KFI61803.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029046}.
FT   DOMAIN          25..397
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          411..620
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   ACT_SITE        161
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        320
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   695 AA;  77475 MW;  F26B790038AEED97 CRC64;
     MNIRRPFRWP NLLTETGRGI AYGGDYNPDQ WPEEVWDEDI RLMTKAGVNT VALAIFSWDR
     IQPAEDTWDF DWLDRIIGKL GKAGIAVDLA SATAAAPLWL YRAHPEVLPV EANGNVVHAG
     SRQSWRPTSP VFREYALTLC RKLAERYKDN PYVTAWHMGN EYGWNNAVDY SDDAVRAFQR
     WCEERYGTPE AVNEAWGAAF WSQEVRSFDE IDVPRHMGAD SMVNPAKQLD YTRFCSDALK
     EFYRTERDAI EEICPDKPFT TNFMVSTDQC TLDYADWSAE VDFVSNDHYF VPGESHLDEL
     ACSDSLVSGF AGHNPWYLME HSTSAVQWKP VNTRKRNGEM VRDALAHVAM GADAVNFFQW
     RQSRSGAEAF HSAMVPHAGP DTTVFREVCD LGVILKRLSD SGVQGTCPVD APTAILFSAG
     AEWATRSRTL PSGQLSHWHD IRDWYRAFLD TGSRADVVPL SADWSGYGTV ILPTVLVLSD
     EDTARLAAFA EDGGRVVVDY ATGIVDDNFR TGLGGYPGAG DGLLRRMLGV RGEEFNILGP
     IDGEPDAVRL SNGAVSRLWQ TVVTSVAADT EIVASYHGAD ASEWQIDGVP AVTRHPYGKG
     EAWYVGCDLD RADIAHLLRF ELARSHACTD PTHRHDPRIL HVARVGEGGR FDWYFNRAKE
     PVEVRVGGEV VVLFRGDDVP GGYVLQRNGV VLVRS
//
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