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Entry: A0A191USP3_9ACTN
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ID   A0A191USP3_9ACTN        Unreviewed;       599 AA.
AC   A0A191USP3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=GCM10010220_66580 {ECO:0000313|EMBL:GGS04973.1},
GN   Spa2297_01275 {ECO:0000313|EMBL:ANJ05729.1};
OS   Streptomyces parvulus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=146923 {ECO:0000313|EMBL:ANJ05729.1, ECO:0000313|Proteomes:UP000078468};
RN   [1] {ECO:0000313|EMBL:ANJ05729.1, ECO:0000313|Proteomes:UP000078468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2297 {ECO:0000313|EMBL:ANJ05729.1,
RC   ECO:0000313|Proteomes:UP000078468};
RA   Nishizawa T., Miura T., Harada C., Guo Y., Narisawa K., Ohta H.,
RA   Takahashi H., Shirai M.;
RT   "Non-Contiguous Finished Genome Sequence of Streptomyces parvulus 2297
RT   Integrated Site-Specifically with Actinophage R4.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GGS04973.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4068 {ECO:0000313|EMBL:GGS04973.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [3] {ECO:0000313|EMBL:GGS04973.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4068 {ECO:0000313|EMBL:GGS04973.1};
RA   Sun Q., Ohkuma M.;
RL   Submitted (DEC-2022) 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|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; CP015866; ANJ05729.1; -; Genomic_DNA.
DR   EMBL; BMRX01000025; GGS04973.1; -; Genomic_DNA.
DR   RefSeq; WP_064726106.1; NZ_CP015866.1.
DR   AlphaFoldDB; A0A191USP3; -.
DR   KEGG; spav:Spa2297_01275; -.
DR   Proteomes; UP000078468; Chromosome.
DR   Proteomes; UP000645274; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675}.
FT   DOMAIN          16..327
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          377..486
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          510..566
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        163
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        239
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   599 AA;  64682 MW;  DEC76DB5194AE697 CRC64;
     MTSSHPPTLT RADGTFLRAG RPHRVLAGSL HYFRVHPEQW ADRLERLAAL GLNTVDTYVP
     WNFHERRPGE ARFDGPRDLP RFARLAQGTG LDVIVRPGPY ICAEWDNGGL PAWLTGTPGM
     RPRTSHGPFL DAVGRWFDVL VPRLAELQAA RGGPVVAVQI ENEYGSYGDD QDYVRRVRDA
     LTGRGITELL YTADGATPLM LDGGSLPGEF AAATFGSRPD VAAALLRARR PGEPFFCAEF
     WNGWFDHWGE KHHVRSSDSA AQDVGEILDA GGSVSLYMAH GGTNFGLWAG ANHDGERLQP
     TVTSYDSDAP VAEHGALTPK FHALRAKLAT VPGAPARERR LPADPPLLPP RTLPVARRAA
     LLDALRAVSE PVRAPVPLGF DELGQSAGLV LYTAHPLLPA GVHEVTVTGL HDRAQVFADG
     VPVAVLDRET AAFPLTGTGD RVRLELLVEN QGRINYGPLL GQGKGILGGV RVERRLVHGW
     TMHPLPLDEW SPHDLARAAS AAGPGGTAGF ATAVLDVPEP ADTFLALPGF AKGFVWAGDT
     LLGRYWEAGP QTTLYLPRPL LRPGPNTLTV LELERLGDHV ALVDRPDLGP TEEYVETFG
//
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