ID A0A1B2HTY1_9PSEU Unreviewed; 662 AA.
AC A0A1B2HTY1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=BBK82_39620 {ECO:0000313|EMBL:ANZ41181.1};
OS Lentzea guizhouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=1586287 {ECO:0000313|EMBL:ANZ41181.1, ECO:0000313|Proteomes:UP000093053};
RN [1] {ECO:0000313|EMBL:ANZ41181.1, ECO:0000313|Proteomes:UP000093053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHS C013 {ECO:0000313|EMBL:ANZ41181.1,
RC ECO:0000313|Proteomes:UP000093053};
RA Cao C.;
RT "Complete genome sequence of the Lentzea guizhouensis DHS C013.";
RL Submitted (JUL-2016) 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}.
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DR EMBL; CP016793; ANZ41181.1; -; Genomic_DNA.
DR RefSeq; WP_065919518.1; NZ_CP016793.1.
DR AlphaFoldDB; A0A1B2HTY1; -.
DR STRING; 1586287.BBK82_39620; -.
DR KEGG; led:BBK82_39620; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000093053; Chromosome.
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:UP000093053};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 18..383
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 395..597
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 607..658
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 154
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 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
SQ SEQUENCE 662 AA; 72082 MW; 5E8C37C022A658C8 CRC64;
MTARRLTYRL GGLAFGGDYN PEQWDEQVWK EDDELMRRAG VNLATVGVFS WALLEPEEGR
YDFAWLDAHL DRLHGNGVAV DLATPTASPP PWFTLAHPDA LPVGPDGTRL VHGSRDTYCL
TAPAYRSAAR RIAAALAERY GDHPALALWH VHNEYTTLCW CEHTAAAFRM WLRARYDSLD
AVNKAWGTAF WSQRYGSWEQ VLPPRATQWH RNPGHALDFR RFFSDEVVAA YTEQRDAIRA
HSDRPVTTNL MMPAYQNVDL WALGREVDVV AIDHYPDRPG LAAAADVAFA ADRARSFAGG
GPWLLMEQGT STVYDHGRVL AKEPGEILRH SLGHIARGSE GALFFQWRQS KAGAEQWHSA
MVPHAGPESR VFAEVAETGG AVARLAPLAG STVTAQVAVL HDSDAWWALS SDGLPSPDLD
YHSALRAAHR AVWDVGVVAD FAHPEADLGR YRLVLAPALY LLSDAGAENL RRYVAGGGTL
LVGHFSGVVD DRAHSRLGGY PATPLREALG IRVEEYRPLR QDERITLSDG SHGTVWSESL
RTRGAEAVVA YTHGALAGSP ALTRYGYGGG EGWYLSTRLD DTAHGALVAR LLDATGVRPA
LPGLPPGVES VTRQGEHDHW HVVLNHTAEP VPLPMTAHDL LTGGPLTALA PGGCAVLRGA
TP
//
