ID   Q0UXG4_PHANO            Unreviewed;       977 AA.
AC   Q0UXG4;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 84.
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=SNOG_03550 {ECO:0000313|EMBL:EAT88755.2};
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT88755.2, ECO:0000313|Proteomes:UP000001055};
RN   [1] {ECO:0000313|Proteomes:UP000001055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC   {ECO:0000313|Proteomes:UP000001055};
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA   Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA   McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445329; EAT88755.2; -; Genomic_DNA.
DR   RefSeq; XP_001794108.1; XM_001794056.1.
DR   AlphaFoldDB; Q0UXG4; -.
DR   STRING; 321614.Q0UXG4; -.
DR   EnsemblFungi; SNOT_03550; SNOT_03550; SNOG_03550.
DR   GeneID; 5970971; -.
DR   KEGG; pno:SNOG_03550; -.
DR   VEuPathDB; FungiDB:JI435_035500; -.
DR   eggNOG; KOG2024; Eukaryota.
DR   HOGENOM; CLU_002346_0_0_1; -.
DR   InParanoid; Q0UXG4; -.
DR   OrthoDB; 276651at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0009341; C:beta-galactosidase complex; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005990; P:lactose catabolic process; IBA:GO_Central.
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; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
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; PF00703; Glyco_hydro_2; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT   DOMAIN          751..970
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   977 AA;  110121 MW;  61CEB39BD2232A9E CRC64;
     MASGTYPAAK PDWNNLDILH ENTLAPRAYF HNYTSEADAL TYDVTKSKIH NLSGTWKFEH
     AYSPFEAPEG FEAPSFDTSK WSDIAVPGMW QLQGFGKGPQ YTNVQYQIPV DPPNVSFTEN
     ETGSYVKKFK IPQELQSGQI RLRFEGVDAA FHVWVNGKEV GYSQGSRNPD EFDITSLVDL
     NGENVLAVRV YQLCDGTYIE DQDQWWLSGI FRDVLLIGFP KESRIDNVFA QTLLDSSYTD
     ADLKVKVSAI GSGKVTVKVL DAQKKIVATA DAEVNNGGST DFSIPVKNPL KWTAESPNLY
     HLVVSLGSEQ FVTQRIGFRQ VEMKDGLIKV NGKRIVFRGV NRHEHHPKHG RTVPLEFLKQ
     DLLTMKRHNI NAIRTSHQLN DPRLYDLADE MGFWVMDEAD LECHGFETIA DLALTPAEQK
     LPFRERQLLT REKAAEWTTD NPDWTKAYVD RAEHLVKRDQ LHPSIISWSL GNEAFYGRNF
     KAMYDHIKAY DNSRPIHYEA DIYAETMDMY SRMYPPINEI IEFGKDKTKT KPLVLCEFVH
     AMGNGPGNIK EYVDAFYEYP TLQGGFAWEW ANHGLVTKDK QTGEEFMAYG GDFGEEVHDS
     TFVMDGLVNS DHTPNAGLVE YKKAIEPVQL LESSKTKAKF INRYDIITLD HLVCQYTVAS
     EAGGEGKSGV LDIPSGIAPG QTFEVELPQI SDLVGEALLS ITFGLKEATP YLEKGFEVGT
     AQIPITATAP VQLPAKSDGK LEVATSRNLL EITSQKSTWK FNTLHGTLTS WRQASTELIT
     KAPEFDIFRA ETDNDAPQDG WEWKEKCLHL AKPSTRKVEW SQPDANTLKV VVNQRLAPPT
     LSWSIDTILT YTFRSNGSVS IAVNGTPRGA NLPRTLPRIG LVMSLPQQFQ RVDWFGRGPG
     ESYRDSKFSQ PVGKYTAQTI DELWVDYEVP QESANRTDTR WVSVSNGKDA LLLAQFVKGE
     ERKLFDFQWE LWTEDAG
//