ID   A0A0F7FYP5_9ACTN        Unreviewed;       975 AA.
AC   A0A0F7FYP5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=SXIM_42950 {ECO:0000313|EMBL:AKG45679.1};
OS   Streptomyces xiamenensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG45679.1, ECO:0000313|Proteomes:UP000034034};
RN   [1] {ECO:0000313|Proteomes:UP000034034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA   Xu J.;
RT   "Complete genome sequence of a mangrove-derived Streptomyces xiamenensis.";
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|ARBA:ARBA00001412};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; CP009922; AKG45679.1; -; Genomic_DNA.
DR   RefSeq; WP_046724898.1; NZ_CP009922.3.
DR   AlphaFoldDB; A0A0F7FYP5; -.
DR   STRING; 408015.SXIM_42950; -.
DR   KEGG; sxi:SXIM_42950; -.
DR   PATRIC; fig|408015.6.peg.4348; -.
DR   HOGENOM; CLU_002346_0_2_11; -.
DR   Proteomes; UP000034034; Chromosome.
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}.
FT   DOMAIN          703..970
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   975 AA;  108099 MW;  E22A592EAD37EB2E CRC64;
     MDTRPAHDGH PYEEDRSPGH GTLPARVWYA ASDAARLSLN GTWAFRLSDT AEGTGTAFTE
     DTADLSDWAR VRVPGHWVLQ GHGAPAYTNI VYPIPVDPPR VPTENPTGDH RLDFDLPGDW
     PQDGETLLRF EGVDSCARVW LNGHELGWFT GSRLPHEFAV GHLLRPRGNV LAVRVHQWSA
     GSYLEDQDMW WLPGIFRDVT LLHRPDGAPC DFFVHAGYDH LTGRGTLRVA CDVAGRILVP
     ELGLDVRVGE ETSAPVEPWS AESPRLYHGE LITAGERVPL RIGFRTVRVE NGVFTANGRR
     ILFRGVNRHE FHPETGRAVD LETMRRDVLL MKRHNINAVR TSHYPPHPAF LDLCDELGLW
     VIDEADLETH GFCYFPDWRG NPVADERWTP ALIDRARRMV ERDKNHPSVV IWSLGNECGA
     GQGLSAMAAW IRERDPSRPL HYENDYSYRD SDFYSRMYAP HDEVEAIGRG EEQPLEDPEA
     DARRRSLPLL LVEYAHAMGN GPGGLADYQR LFETYERCQG GFVWEWIDHG LPKRTADGRP
     YYAYGGDFGE DVHDGNFVCD GLLFPDRSPS PGLIEYKKVI EPVRITGDSA AGTITVTNRH
     DFSALDHLSF TWAFEVEGEE TATGTLAVPS LDPGTSAVVP LPDPPHARAG EAVWTIRAGL
     RADTPWAPRG HLVAWAQLPA RPRPLPERPA VLLPPLAEAG NIHLGPAVFH ATTGELRSLN
     GLDLRQGPRL DVWRAPTDND LGGPWLGDAR LAMRWRKLGL HRLQHRVDSI STADRALTVR
     TRVAPAATDL GLYAAYHWSA DDERLLLTVT VTPDGEWPVP LPRLGLLLGL PASCDHATWY
     GGGPGEAYPD TRAASRLGRY SMNVDDMQTP YVRPQENGAR PDVRWAELCA AGGPGLRVTA
     GDAPFWFTAR RWSDVQLDAA RHTTDLEPGD TVWVHLDRSV QGIGTESCGP GPLPQYRLTV
     APTTFSLVLT APGAN
//