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
//