ID A0A420EZU3_9ACTN Unreviewed; 667 AA.
AC A0A420EZU3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-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=D7I43_16755 {ECO:0000313|EMBL:RKF26233.1};
OS Micromonospora globbae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1894969 {ECO:0000313|EMBL:RKF26233.1, ECO:0000313|Proteomes:UP000285744};
RN [1] {ECO:0000313|EMBL:RKF26233.1, ECO:0000313|Proteomes:UP000285744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WPS1-2 {ECO:0000313|EMBL:RKF26233.1,
RC ECO:0000313|Proteomes:UP000285744};
RX PubMed=29458491; DOI=.1099/ijsem.0.002625;
RA Kuncharoen N., Pittayakhajonwut P., Tanasupawat S.;
RT "Micromonospora globbae sp. nov., an endophytic actinomycete isolated from
RT roots of Globba winitii C. H. Wright.";
RL Int. J. Syst. Evol. Microbiol. 68:1073-1077(2018).
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:RKF26233.1}.
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DR EMBL; RAQQ01000011; RKF26233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420EZU3; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000285744; 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:UP000285744};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 14..383
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 395..596
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 605..660
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 149
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 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 667 AA; 73669 MW; 69F627DFBD18E2DE CRC64;
MRRWQGDRIL FGGDYNPEQW PEETWAEDVE LMRRAGVNLV SVGIFSWALL EPAPGRYEFG
WLDRVLDLLH AGGVDVDLAT ATASPPPWLA RAHPETLPRR ADGTVLWPGG RQAYCPSSPV
FRERSLALVE AVAGRYAAHP AVVMWHVSNE LGCHNVHCYC DVSAEAFRAW LRERYGDLDA
LNAAWGTAFW SQRYGDWAEI NPPRTAPTFA NPTQQLDFLR FSSDEQRAQL RAEREVLRRL
VRQPVTTNFM IGTGVKYLDY HSWAGDVDLV ANDHYLTAAD PRAHVGLALS ADHTRGVAGG
EPWLLMEHST SAVNWQPRNV AKTPGQLRRN SLAHVARGAD GVLFFQWRAS RAGAEKFHSA
LVPHAGPDTK VFREVCRLGA DLGALAEIRG SRVEADVAIL FDYEAWWGVE LDSHPSVDVT
YLDRLTALYD SLWRAGITAD VVHPSTDLAR YRLVLAPTLY LVRDADAAAL RRFVTDGGTA
LVTYFSGIVD EHDHIRLGGY PGAFRDLLGV RTEEFFPLRE GERVRLDDGS VADVWTEWLH
PDGAEVLASY VDGPLPGVPA LTRHEVGAGA AWYAGTRLDQ SATDRLVGRL VAESGVRPAA
VAPEGVEVVR RRDGERSWLF VVNHTTGPAR VPVTGVELLT RDRCDGEVVV PAGEVAVVRE
DPDATTA
//
