ID A0A136IUJ9_9PEZI Unreviewed; 956 AA.
AC A0A136IUJ9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=Micbo1qcDRAFT_166515 {ECO:0000313|EMBL:KXJ88479.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ88479.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) 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, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; KQ964258; KXJ88479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136IUJ9; -.
DR STRING; 196109.A0A136IUJ9; -.
DR InParanoid; A0A136IUJ9; -.
DR OrthoDB; 276651at2759; -.
DR Proteomes; UP000070501; 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; 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.
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, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000070501}.
FT DOMAIN 664..956
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 956 AA; 108727 MW; 73AED3E82688820E CRC64;
MQGFGKGPQY TNVNYPFPVD PPNVPFDDNE CGRYVTNFEV GPSIKDGKQF RLRFEGVDAA
FSAWLNGKYV GYSQGSRNPS EFDVTKSLKF DGEENTLCVE VYQRCDGSYI EDQDQWWLNG
IFRDVWLHSF PETHFQDFYV QTLLNDDFQD ARLHVETTVS KSHQGVRLKL FDAENEVVAE
SSNEQLSVMR STAQKTVSQD LDIKKPHKWT AETPYLYTLI LEVDGLYTSH KIGFRRAELV
DGVFCVNGNP VKIRGVNRHE HYPSSGRTVP YEFMRRDLRT MKLFNINAIR TSHYPNDPRL
YDVANEFGFW VIDEADLECH GFENAGGVPA SYTSDNPEWE EAYLDRARQL VARDKNHPCV
IMWSLGNEAF YGRNHQAMYD EMKRMDPTRL IHYEQDYDAQ TADVFSRMYT SVGDMIKFGE
EKDWKKPFVM CEFGHAMGNG PGGLKEYIDA FYKYPRLMGG FIWEWANHGL LTKNADGEEY
FGYGGDFGDE PNDGNFVMDG LCDSNHNQGP GLNNYSALIQ PVQIVGMKGL DIEIVNRYDF
LTLDHLSCYW NIIRDRSQVI GREIVIPKGV KPHSIVTINL ANDFPIETLK DGIAILELEF
IQKDAPGWAY PNHTAARCQV EMHPPKSLAL LKSISSTNTG TSAGINNTFP QISTSSDGLF
HRVTLSNDKT FGFDKSKGTL SFMAYSSAAN AENLITEPFT LDFYRALTDN DRPVFGQDWL
DARLHQTRQH FTSMTTSAVA PSTTNGGRPE CSVTIHARVA PPVLAWAVDT ITTYTFTPET
CCIRVQAKPH GPFLPSTFAR FGLSFGIKDV SIAEWFGRGP EQSYCDFKDA QLVNTWGWTV
DGMWQDYEFP QDNGNRSDVS WVELRKQWGG DADGRTLRAR FGDFQGASFT VSRYTTRDID
EARHPWELHK TRRDGDVLVR LDWHHHGLGT GSCGPATLPE YQLRTDREFD VEVLLD
//
