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Database: UniProt
Entry: C4FDD5_9BIFI
LinkDB: C4FDD5_9BIFI
Original site: C4FDD5_9BIFI 
ID   C4FDD5_9BIFI            Unreviewed;       707 AA.
AC   C4FDD5;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=BIFANG_02318 {ECO:0000313|EMBL:EEP20966.1};
OS   Bifidobacterium angulatum DSM 20098 = JCM 7096.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=518635 {ECO:0000313|EMBL:EEP20966.1, ECO:0000313|Proteomes:UP000006408};
RN   [1] {ECO:0000313|EMBL:EEP20966.1, ECO:0000313|Proteomes:UP000006408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20098 {ECO:0000313|EMBL:EEP20966.1,
RC   ECO:0000313|Proteomes:UP000006408};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2009) 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:EEP20966.1}.
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DR   EMBL; ABYS02000004; EEP20966.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4FDD5; -.
DR   STRING; 1683.Bang102_002335; -.
DR   PATRIC; fig|518635.7.peg.291; -.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_012430_1_1_11; -.
DR   Proteomes; UP000006408; 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};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084}.
FT   DOMAIN          42..414
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          429..632
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          650..707
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        178
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        337
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   707 AA;  79244 MW;  A6D2186EC8E19DFA CRC64;
     MLRLELRRGV ASKRRKSMTQ RRAFHWPQPL EGQQARIWYG GDYNPDQWPE EVWDEDVRLM
     KKAGVNLVSV GIFSWARIEP REDVYDFDWL DRIIDKLGKT GIAVDLASAT ASPPMWLTQA
     HPEVLWKDYR GDVCQPGARQ HWRPTSPIFR EYALKLCRAM AEHYKDNPYV VAWHVSNEYG
     CHNRFDYSED AERAFQQWCK ARYGTIDAVN DAWGTAFWAQ HMNDFSEIVP PRFIGDGNFM
     NPGKLLDFKR FSSDALKAFY IAERDTLAEI TPGRPLTTNF MVSSGNTTVD YDDWGNEVDF
     VSNDHYFTPG EAHLDELAFS ASLVDGIARK DPWFLMEHST SAVNWRPINY RKEPGQLVRD
     SLAHVAMGAD AVCYFQWRQS KAGAEKFHSA MVPHAGEDSQ TFRDVCELGA DLNTLADNGL
     LGTRLAKSRV AVVYDYESEW ASEHTATPTQ QVHHIDEPLQ WFRALADNGV TADIVPVRSN
     WDEYEVAVLP SVYILSEETT RRVRDYVANG GKLIVTYYTG LSDEKDHIWL GGYPGSIRDV
     VGVRIEEFAP LGTDWPGTAD HLDLSNGAVA HDFADVITSV GKNATVLASF QDDPWTGMDG
     RPAIVGNTYG EGRSVYVGAR LGRDGIAKSL PAVFASLGVE AADASDPRLL RVERKDEATG
     TKFTFLFNRT HGPVETSEEG EPIVTSLAKA DGGKLTIGPN GVVVVKR
//
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