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Database: UniProt
Entry: A0A0C5FLK0_9ACTN
LinkDB: A0A0C5FLK0_9ACTN
Original site: A0A0C5FLK0_9ACTN 
ID   A0A0C5FLK0_9ACTN        Unreviewed;       591 AA.
AC   A0A0C5FLK0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-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=TU94_02880 {ECO:0000313|EMBL:AJP00617.1};
OS   Streptomyces cyaneogriseus subsp. noncyanogenus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP00617.1, ECO:0000313|Proteomes:UP000032234};
RN   [1] {ECO:0000313|EMBL:AJP00617.1, ECO:0000313|Proteomes:UP000032234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP00617.1,
RC   ECO:0000313|Proteomes:UP000032234};
RA   Wang H., Li C., Xiang W., Wang X.;
RT   "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp.
RT   Noncyanogenus NMWT1, the producer of nematocidal antibiotics nemadectin.";
RL   Submitted (FEB-2015) 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; CP010849; AJP00617.1; -; Genomic_DNA.
DR   RefSeq; WP_044378936.1; NZ_CP010849.1.
DR   AlphaFoldDB; A0A0C5FLK0; -.
DR   STRING; 477245.TU94_02880; -.
DR   KEGG; scw:TU94_02880; -.
DR   PATRIC; fig|477245.3.peg.641; -.
DR   HOGENOM; CLU_007853_7_2_11; -.
DR   OrthoDB; 9813184at2; -.
DR   Proteomes; UP000032234; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032234}.
FT   DOMAIN          11..324
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          370..481
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          505..563
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        159
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        235
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   591 AA;  64073 MW;  1357C5783617D4F7 CRC64;
     MPALTTTSGG FLLNGEPFRI VSGALHYFRV HPEQWADRLR KARLMGLNTV ETYVPWNLHQ
     PDPEGPLVLD GLLDLPRYLR LAGREGLRVL LRPGPFICAE WDGGGLPAWL TADPDIRLRS
     SDPRFTDAVD RYLDLLLPPL LPHFAGSGGP VIAVQVENEY GAYGDDTAYL RHLADALRAW
     GVEELLFTCD QADPAHLVAG SLPGVLATGT FGSRIEQSLA RLRAHQSEAP LMCTEFWVGW
     FDHWGGPHHV RDAADAAADL DRLLSAGASV NLYMFHGGTN FGFTNGANHH HAYAPTVTSY
     DYDAPLTEWG DPGPKYHALR EVIARHAPVP DEPVPSPGRK LPPTEVVLDR RAPLLPHASA
     LGAPVRAEDP LTMQALGQRA GFALYRTSVP RSGDGLLRFA GGVGDRAQVF VDGAPAGVLE
     RERRDETLPV RIPRPGATLE VLVENMGGVN YGPHIGTPKG LLGPVSFEDT VLRGWDCHPL
     PLDGPDGPAG TLPFVPSGQV TSAVPAFHHG RFRVEEPADA FLALPGWTKG QAWINGFPLG
     RYWNRGPQRT LYVPAPVLRP GANELLLLES HGTTSARVLL TDTPDLGPVR S
//
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