ID A0A0D8HL69_9ACTN Unreviewed; 673 AA.
AC A0A0D8HL69;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 Name=bgaB {ECO:0000313|EMBL:KJF18750.1};
GN ORFNames=AXFE_03590 {ECO:0000313|EMBL:KJF18750.1};
OS Acidithrix ferrooxidans.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidithrix.
OX NCBI_TaxID=1280514 {ECO:0000313|EMBL:KJF18750.1, ECO:0000313|Proteomes:UP000032360};
RN [1] {ECO:0000313|EMBL:KJF18750.1, ECO:0000313|Proteomes:UP000032360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Py-F3 {ECO:0000313|EMBL:KJF18750.1,
RC ECO:0000313|Proteomes:UP000032360};
RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT "Draft genome of the acidophilic iron oxidizer Acidithrix ferrooxidans
RT strain Py-F3.";
RL Submitted (JAN-2015) 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:KJF18750.1}.
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DR EMBL; JXYS01000007; KJF18750.1; -; Genomic_DNA.
DR RefSeq; WP_052604171.1; NZ_JXYS01000007.1.
DR AlphaFoldDB; A0A0D8HL69; -.
DR STRING; 1280514.AXFE_03590; -.
DR PATRIC; fig|1280514.3.peg.493; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000032360; 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:0005975; P:carbohydrate 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 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; 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; 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, ECO:0000313|EMBL:KJF18750.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:KJF18750.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000032360};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 21..390
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 402..604
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 313
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 165
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 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 673 AA; 74856 MW; D53B5F73141F9BD1 CRC64;
MTVYSERLSL PLGRPLYFGG DYNPEQWSRD VWQQDVEMMV EAGVNLVTLG VFSWSRLQSA
PGKFDFGWMD EIFELLSSNG IMVDLATATA SPPPWLVHAH PEILPRDFSG RTLSFGSRQS
YCPNSRPYRD AAAELVHALA QRYGSHSALE MWHINNEYGC HVTSCYCDVC EVAFREWLVK
RYVDIAGLNF AWGTTFWSQI YTDWNQVTPP RIAPTFSNPT QQLDYARFSS DSLLDCLLEE
RAILREVTPQ IPVTTNFMGF FKGVDQFKWA EALDFCAVDN YPDPASPTSS LISGAVGDLT
RSVGQGRPWI LMEQAPSAVN WREINAPKAP GQNRALSMSS IARGANGVMY FQWRAAKAGA
EKFHSAMVPH SGRNSRVWRE TVRLGNDLKA LGSLGSSQTL VDVAILFDWD NWWAIELDSH
PSTKLSYPLG ILDLYRSFAR AGRVVDFVHP GSDLSRYKVV VAANLYLVKE DASCAFVEYV
QNGGVGVVTY FSGIVDENDH VYLGGYPGLW RELLGIEIEE FSPLAIGESV SLKGEFLQLH
GGSGQQWSDS INLVGAEVLV SFGSGRLEGM PAITKNAFGS GKAYYVSTSL DPDTWGLVLT
DALSGHEEIA IRPSSEDVEI VNRGNLVFII NHGLKTNLSL EGDWIDVLTK CEVSGELSLE
QYDVYVLYRL IRE
//
