ID A0A1U9QMK0_STRNV Unreviewed; 672 AA.
AC A0A1U9QMK0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=BBN63_03890 {ECO:0000313|EMBL:AQU65514.1};
OS Streptomyces niveus (Streptomyces spheroides).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=193462 {ECO:0000313|EMBL:AQU65514.1, ECO:0000313|Proteomes:UP000189677};
RN [1] {ECO:0000313|EMBL:AQU65514.1, ECO:0000313|Proteomes:UP000189677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 3406 {ECO:0000313|EMBL:AQU65514.1,
RC ECO:0000313|Proteomes:UP000189677};
RA Zhu Q., Cheng W., Song Y., Li Q., Ju J.;
RT "Complete genome sequence of Streptomyces niveus SCSIO 3406.";
RL Submitted (NOV-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; CP018047; AQU65514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9QMK0; -.
DR KEGG; snw:BBN63_03890; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000189677; 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 Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 22..392
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 405..596
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 610..664
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 158
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 316
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 672 AA; 73896 MW; 1812BB7836096A1C CRC64;
MPRPDEPHPA WGRVPRPAFG ADYNPEQWDR ATWHDDVRLM REAEVNLVSL GIFAWSWVEP
RPDTFDFTGL DEVVALLHGA GVAVDLATPT AAPPLWFSHA HPESLPVTAD GRRLAPGSRQ
AYCPSSPAYR ARAALITRRL AERYGDHPAV VMWHINNEYA NGNAHCWCET SAGAFRGWLR
TEYGDDLDAL NDRWGRSVWG MRYSDWEQVT VPRTSTSSLS PGLWMDFYRF SDAEHLACFR
AERDIVRGHS PGRPVTTNFM TGKLGWTDYW RWAREVDIVS NDHYLMSEDP DRGADLALAA
DLTRGLAGGR PWMIMEHSTS AVQWQPRNVA KAPGEMARNT LTHLARGADG ALFFQWRQSA
HGPEKWHSAM VPHGGEETRI WREAKALGNT VAALADIAGS ICPPAEIALL LDYEAMWALE
LPHRPSTDLT YSGVLRDWHR ALWTLGLFCD LVPTPGEQRL LLVPSLYALS TDTARALEEY
AARGGHLVVG PFSGLTDPDD RVHPGPYPGA LRDLLGLRVD EYLPLAAGEA VHLDDGSTGH
LWAERVVPAP DTEVEARFTD GPAADGPATV RHGNVRYLAT RPDASSLLRL LPLWAAQAGC
APAPEEAGQG VEVVRRTAPG DRTWLFAVNH TRHPVRVAAT GVDLLTGVRS SGTITLPAGE
VAVVAEDSPV TP
//
