ID A0A3S0CTD9_9BACL Unreviewed; 692 AA.
AC A0A3S0CTD9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=EJQ19_17680 {ECO:0000313|EMBL:RTE08259.1};
OS Paenibacillus whitsoniae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2496558 {ECO:0000313|EMBL:RTE08259.1, ECO:0000313|Proteomes:UP000276128};
RN [1] {ECO:0000313|EMBL:RTE08259.1, ECO:0000313|Proteomes:UP000276128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MER 54 {ECO:0000313|EMBL:RTE08259.1,
RC ECO:0000313|Proteomes:UP000276128};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus ochoae sp. nov., Paenibacillus whitsoniae sp. nov., Paenibacillus
RT spiritus sp. nov. Isolated from the Mars Exploration Rover during
RT spacecraft assembly.";
RL Submitted (DEC-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:RTE08259.1}.
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DR EMBL; RXHU01000054; RTE08259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0CTD9; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000276128; 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:UP000276128};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 19..392
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 403..614
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 626..680
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 314
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 692 AA; 79983 MW; A5EE6F1A5E37733A CRC64;
MSQRKPLFPQ LNRMLHGADY NPEQWIHMPE VWDEDMRLMR LAKCNVMTMG MFSWSSLEPK
EGQFEFGWLD EIIDKLTRNG ISFILGTPSG ARPAWLASKY PEVLRVRPER VRNLYGTRHN
HCYTSPVYRE KVRIINTLMA ERYGGHPDLL LWHISNEYNG ECHCDLCQAA FREWLKKKYN
DDLDRLNQMW YTTFWSHTYT DWKEIESPSP IGEHMLHGLQ LDWKRFVTDQ SIDFMLQEIA
PLKRLTPDIP VTTNFLGGCN INYEKMAEQV DIVSWDSYPY WHSKDPDWKT ACHAAFTHDR
YRSFKPDKPF LLMECTPSLA NWQEVAKLKR PGMHALSSIQ AVAHGSDSVQ YFQWRKSRGS
SEKFHGAVVD HSAHEHTRVF REVAELGADL ERLQPVNGTI IRAETALIYD TENKWVVEGA
AGPRKPNLSY DQEVFRHYEP FWKQGIPVDI ISMDRSLEGY KLVIAPMLYM LKQGTAERFE
TFVRSGGTLV LTYWSGIVDE NDLCFLGGFP GPLRKLAGVW SEELDALYPE DHNALIMKEN
ALEGLSGSYS VSLMCDLIHV ETAKVLAEYQ EDFYQGYPAL TLNRFIDGEV YYIAARTEPS
FLEDFYLVLA DRYRLGRALH ADWAEGVNAQ VRTDGDRAYI FLHNFTNKEQ NILLKESVTD
LDGTPVDQHL ILPAYGYRVF IRDGNDGSNA NA
//
