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Database: UniProt
Entry: A0A101TC94_9ACTN
LinkDB: A0A101TC94_9ACTN
Original site: A0A101TC94_9ACTN 
ID   A0A101TC94_9ACTN        Unreviewed;       965 AA.
AC   A0A101TC94;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=AQJ66_01405 {ECO:0000313|EMBL:KUN89763.1};
OS   Streptomyces bungoensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN89763.1, ECO:0000313|Proteomes:UP000053024};
RN   [1] {ECO:0000313|EMBL:KUN89763.1, ECO:0000313|Proteomes:UP000053024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN89763.1,
RC   ECO:0000313|Proteomes:UP000053024};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT   for the species Streptomyces bungoensis.";
RL   Submitted (OCT-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|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:KUN89763.1}.
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DR   EMBL; LMWX01000003; KUN89763.1; -; Genomic_DNA.
DR   RefSeq; WP_061915119.1; NZ_KQ948851.1.
DR   AlphaFoldDB; A0A101TC94; -.
DR   STRING; 285568.AQJ66_01405; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000053024; 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   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; IPR008979; Galactose-bd-like_sf.
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; IPR006104; Glyco_hydro_2_N.
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; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 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   SUPFAM; SSF49785; Galactose-binding domain-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:UP000053024}.
FT   DOMAIN          695..954
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   965 AA;  106246 MW;  504FD370147576B1 CRC64;
     MTFRTRTRTR TDYVEDVAPG DGALPPRAWY ASSDARSLSL NGSWRLRVSG TADAEDDSFA
     AQGYDAGDWA EVPVPGHWVL QGHGSPAYTN HLYPFPVDPP RVPTENPTGD HLRVFDLPAD
     WPDLAEGGAV LRFDGVESCA RVWLNGTELG TFKGSRLPHE FAVGHLLKPA GNVLAVRVHQ
     WSSGSYLEDQ DQWWLPGIFR DVTLLHRPAG SALDFFVLAA YDHVSGEGTL RVDSDVAGRV
     TVPELGIDTA TGEPVTVPVE PWSAEVPRLY DGVLATEGER IPLRVGFRTV ELSDGLIKVN
     GRAVLFKGVN RHEWHPRHGR ALDPATMRED VLLMKRHNVN AVRTSHYPPH PAFLDLCDEL
     GLWVIDECDL ETHGFTEQAW RDNPVDDDRW TPALLDRAAR MVERDKNHPS VVMWSLGNEA
     GTGRGLTAMA EWIRGRDSSR LVHYEGDPDC RDTDVYSRMY AGHAEVERIG RGLDGGNLKR
     RRLPFILCEY AHAMGNGPGG LADYQRLFET YDRLQGAFVW EWIDHGIEDQ RFGYAYGGDF
     GEELHDGNFV CDGLLFPDRR PSPGLVEYKK VIEPVAVEGD GTGGSVRVTN KYDFADLSAL
     AFTWSYEVNG EPVESGALTV PALAPGESAE VKLPEPPVAT AAGEAHWTVR AELAADAPWA
     PRGHVVAWGQ FAVSPRRAPS VASTARPVPG DGLITLGPAS FDTRTGALRA VGPVAVDGLR
     LDVWRATTDN DDGAAWQTDT RYGPLWRRLG LHRMRHRLDA VEPGEDALTV RTRVAPAACE
     IGLSTVYRWT SDGERLRLAV SVRPEGDWTV PLPRLGIRFA LPAADRVQWY GGGPGEAYPD
     SRTASLIGRW QSTVDELQTP YVRPQENGAR ADVRWAELGG LRIEGDPEFF LTARRWTTEH
     LDAAAHRTDL APGGAVWVNL DHRQHGLGSQ SCGPGPLPRY HLRAEPAAFS FVFSQAGWPS
     PASER
//
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