ID A0A417CXH0_9FIRM Unreviewed; 674 AA.
AC A0A417CXH0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=DW904_08230 {ECO:0000313|EMBL:RHT00492.1};
OS Ruminococcus sp. AM42-11.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=2292372 {ECO:0000313|EMBL:RHT00492.1, ECO:0000313|Proteomes:UP000284976};
RN [1] {ECO:0000313|EMBL:RHT00492.1, ECO:0000313|Proteomes:UP000284976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM42-11 {ECO:0000313|EMBL:RHT00492.1,
RC ECO:0000313|Proteomes:UP000284976};
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:RHT00492.1}.
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DR EMBL; QUIO01000011; RHT00492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417CXH0; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000284976; 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:UP000284976};
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 399..609
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 620..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; 76677 MW; 2272F94C794147B2 CRC64;
MARKIEYGHM LHGGDYNPEQ WLDRPDILKK DIEYFKKAHI NTVSVGIFSW AVLEPEEGKY
NLGWLEEIID NLYKEGISTI LATPSGARPK WMADKYPEVL RMDPDRTRRF FGGRHNHCYT
SPVYRQKVHD MDKLLSQRLG SHPGVILWHI SNEFGGECYC PLCQQKFREW LKEKYGTIEK
LNSSWCTTFW SHIYNSFDQI EAPSPKGENE LHALKLDWNR FVTDRTIDFI KGEVAAIREG
GSELPVTANL MYDYNGLDYK KFRDVLDVVS WDNYPSWHKK EEFFTAIDAG MQHDLMRSIK
NQPFLLMESC PSATNWKPIN KLKKPGMMLA ASLQAVAHGS DSVLYFQLHQ SQGASEKFHG
AVIDHYGGED TRVFKEVTEV GEAMEALKEV CGSQMKSPAA VLYDRENNWA IQDAQGPRNE
NMFYTEAVQK QYRALREQGL NVDVISMEHE LSGYKIVAAP MAYMFKDGYE EKLRAYAENG
GTLVITYWTG LVDGTDKCFL GGTPYGLMEA AGLRTTEIDA LYDWEENHGI SEPGNHLGIS
GTYTCKNLCE LVKVSDAEVL MRYGDDFYAG APVVTHKAYG KGHVYYVGAD MEQAFYSDFY
GKAAKEAGIQ APLGFVPAEV SVTLRENQEN EYLFIQNYAR ETKAVPVPAE YEVIYGAADE
IMQPLATRVL KKKK
//