ID A0A373NP69_9FIRM Unreviewed; 674 AA.
AC A0A373NP69;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=DWZ38_05225 {ECO:0000313|EMBL:RGF76184.1};
OS Ruminococcus sp. AF31-8BH.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=2293174 {ECO:0000313|EMBL:RGF76184.1, ECO:0000313|Proteomes:UP000262205};
RN [1] {ECO:0000313|EMBL:RGF76184.1, ECO:0000313|Proteomes:UP000262205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF31-8BH {ECO:0000313|EMBL:RGF76184.1,
RC ECO:0000313|Proteomes:UP000262205};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RGF76184.1}.
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DR EMBL; QTVN01000003; RGF76184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A373NP69; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000262205; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000262205};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 15..386
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 398..609
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 619..672
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 674 AA; 77234 MW; 45D8B68953417405 CRC64;
MAKKIEYGRF LHGGDYNPEQ WLDRPDILKK DIEYFKEAHI NTVSVGIFSW AVLEPEEGKY
NLDWLEQIID NLYKERIYTI LATPSGARPK WMADKYPEVL RMDPDRTRRF FGGRHNHCYT
SPVYREKVHA IDKLLSQRLG SHPGVILWHI SNEFGGECYC PLCQQKFREW LKEKYGTIEK
LNSSWCTTFW SHTYNSFDQI EAPSPKGEDA LHALNLDWKR FVTDRTLDFI KEEISAIREG
GSELPVTANL MYDYNGLDYK KFRDVLDVVS WDNYPGWHKK EEYLTAIDAG MQHDLMRSIK
KQPFLLMESC PSATNWKPIN KLKKPGMMLA ASLQAVAHGS DSVLYFQLHQ SQGASEKFHG
AVIDHYGGDD TRVFKEVTEV GEALVKLQEV CGSQMKAPAA VLYDRENNWA IQDVQGPRNE
NMFYTEAVQK QYRALREQGL NVDVISMEHD LSDYKIVAAP MAYMFLDGYE KQLRTFAENG
GTLVLTYWSG LVDGTDKCLL GGTPYGLMEA VGLRTEEIDA LYDWEENFGI PENGNHLGIT
GTYTCKNLCE LVKVSDAEVL MRYGKDFYAG RPVLTHRAYG KGHVYYVCAD MEQAFYEDFY
GRTVKEAGVQ APLEFVPAGV SVTLRENEAY QYLFIQNFAR EPKAVPVPAG YEVLYGTEKE
VLAPLETRIL KRSK
//