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Database: UniProt
Entry: A0A2N3XSV3_SACSN
LinkDB: A0A2N3XSV3_SACSN
Original site: A0A2N3XSV3_SACSN 
ID   A0A2N3XSV3_SACSN        Unreviewed;       631 AA.
AC   A0A2N3XSV3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=A8926_1325 {ECO:0000313|EMBL:PKW13768.1};
OS   Saccharopolyspora spinosa.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=60894 {ECO:0000313|EMBL:PKW13768.1, ECO:0000313|Proteomes:UP000233786};
RN   [1] {ECO:0000313|EMBL:PKW13768.1, ECO:0000313|Proteomes:UP000233786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44228 {ECO:0000313|EMBL:PKW13768.1,
RC   ECO:0000313|Proteomes:UP000233786};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 Actinobacteria strains.";
RL   Submitted (DEC-2017) 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}.
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:PKW13768.1}.
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DR   EMBL; PJNB01000001; PKW13768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3XSV3; -.
DR   STRING; 994479.GCA_000194155_04043; -.
DR   OrthoDB; 9813184at2; -.
DR   Proteomes; UP000233786; 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          46..362
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          422..533
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          550..608
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        194
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        270
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   631 AA;  69484 MW;  3C3714DE9553D268 CRC64;
     MGVNRRGFPG SIALGGLALG SSMVVGTNRV VAQAQQPAGL TVRGDQFLLD GEPFRIVAGE
     MHYFRTHPDH WRDRLARMRA LGLNTVDTYV AWNFHEPRRG AVDFSSWRDL VRFVETAAEV
     GLKVAVRPGP YICAEWDFGG LPAWLLADPD LPLRCDETAY PDLVDEWFGV LLPRLAPLQA
     TRGGPVIAFQ VENEYGSYAN DQAHLDHLRK TMRDNGIDSL LYCSNGPSEW MLRGGNLPDV
     LATVNFGGDP TEPFAALRRY QPEGPLWCTE FWDGWFDHWG EPHHTTDPVE TAADVEKILA
     AKASVSLYMA VGSTNFGWWA GANFDEANGT YQPTITSYDY DAPIGEAGEL TTKFHRIREV
     IARHEPVPDE PLPPLPSRLP AQRVQPDATV GLLESLDALS ASSIEIEGST SMEIAPIHRS
     APVHMEALGQ PYGLIHYRTH VQGPRETAGL WVRGLADRAL VFADGELLGT LDRNDPQGSV
     EVPVQRESVQ LDLVVDTGGR INFGQRLNDP KGITDRVLHG SQALFGWEIR PLPLDDLSGL
     GFRPGATSGP AFHRAVLRIG APADGFLALP GWEKGMVWLN GFLLGRYWSV GPQRTLYAPS
     PLWRTGENEL IVLELHRRGG STELRSEPDL G
//
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