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Database: UniProt
Entry: S4MKW1_9ACTN
LinkDB: S4MKW1_9ACTN
Original site: S4MKW1_9ACTN 
ID   S4MKW1_9ACTN            Unreviewed;       706 AA.
AC   S4MKW1;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE   AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN   ORFNames=STAFG_8813 {ECO:0000313|EMBL:EPJ34102.1};
OS   Streptomyces afghaniensis 772.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ34102.1, ECO:0000313|Proteomes:UP000015001};
RN   [1] {ECO:0000313|EMBL:EPJ34102.1, ECO:0000313|Proteomes:UP000015001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=772 {ECO:0000313|EMBL:EPJ34102.1,
RC   ECO:0000313|Proteomes:UP000015001};
RA   Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA   Goodfellow M., Mueller M.;
RT   "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT   Compounds of the Julimycin B-Complex.";
RL   Submitted (FEB-2013) 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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:EPJ34102.1}.
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DR   EMBL; AOPY01001716; EPJ34102.1; -; Genomic_DNA.
DR   AlphaFoldDB; S4MKW1; -.
DR   PATRIC; fig|1283301.3.peg.8744; -.
DR   HOGENOM; CLU_002346_0_0_11; -.
DR   Proteomes; UP000015001; Unassembled WGS sequence.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032312; LacZ_4.
DR   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF16353; LacZ_4; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015001}.
FT   DOMAIN          449..704
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   706 AA;  77429 MW;  1C750F40CE3A409E CRC64;
     MPDVRTWTAE TPELYGLTVR LHRADGTVAD SSHHRTGFRD VEIIGRDLLV NGERVFIRGV
     NRHDFHPLTG RTVSYDDMRA DLVLLKRFGF NAIRTAHYPN DPALYDLADE LGFYVVDEAD
     IESHDHAHEI ADDPRYLGAF VDRVARMVLR DKNHPSVIIW SLGNESDYGA NHDAAAGWVR
     RHDPTRPVQY EGAAKRGWAD PDLASDIACP MYAPLQECLA HAMSGTQTKP LIQCEYSHAM
     GNSNGTLADH WEAIEATPGL QGGFIWEFWD HGILQRVNDG RPAGRGGAGL YDNGVAAPGH
     RWAYGGDFGE TDHDGAFIAD GVVFPDRTPK PVMFEHREIA APLRIECFRH EGVVLGNHQH
     FRGLDWLSGE WQLALADGGT RTAPAELPDL RPGETAAVPL PFELPEDGGE AWLTLRVTTA
     RDEPWAPRGT VVCLPQVRLR HAPPTRHAPV THRAVEVDED GLLVHPLLTA GPTLSLWRAP
     TDNDELGGMA ARWRDWGLDA LTRKVVAVRR DPGRVAVVSD HLGPGGTVRH EQVFTAVEGG
     LLVEECAELP EALDDVARVG SVFETAAGLN LLEWFGQGPW ESYPDRGAGA PVGHHSLPVD
     ELFTPYLRPQ ESGGRHGVRR FTLSAPDATG LAVRLDRPRQ VCVTRHRAAD LASAAHPDEL
     VSRAGCVVHI DAAHRGLGTA SCGPDTFASY LVAAGVHRWS WTLRVL
//
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