ID A0A094I7L7_9PEZI Unreviewed; 1026 AA.
AC A0A094I7L7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=V502_02429 {ECO:0000313|EMBL:KFZ23092.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ23092.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ23092.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFZ23092.1}.
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DR EMBL; JPKE01000918; KFZ23092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094I7L7; -.
DR STRING; 1420915.A0A094I7L7; -.
DR HOGENOM; CLU_002346_0_2_1; -.
DR OrthoDB; 276651at2759; -.
DR Proteomes; UP000029308; 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; 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; 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:UP000029308}.
FT DOMAIN 750..1026
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1026 AA; 115762 MW; 237ECF190F0921E8 CRC64;
MASTFPANIP NWNNLSVIHQ NTLPPRASFL PYRNEEDALS HEISKATVQS LSGTWKFKLA
NSPFEAPEDF QLPEHDVSDW APIQVPGMWQ LQGHGKGPQY TNVIFPFPVD PPNVPFDNNE
TGSYVRTFRV LEPFRDHQQR LRFEGVDSAF NVWVNGKHVG YSQGARNPSE FDISNVVDVN
GENTLAVQVY QWCDGSYIED QDQWWLSGIF RDVALVAFPK VHIKDFHVQT LLDDKYQNAV
LSVDVELSSS AKVLLNLRDK DNTIVTSASE SSDGSHVEFR IPIKNPHKWT AETPYLYHLS
LSVDDCSIAS YVGFRKLELR DGLFLVNGKR IVFRGVNRHE HHPSTGRTVP LEFLEKDLLL
MKTHNINAIR TSHQPSDPRL YDLADRLGLW IMDEADVECH GFSHVDDAAL NDEQKKLSFE
EKKALTYGQA ARWTSDNPAW EEAYVDRAKQ LVMRDKNHAS VIMWSLGNEA FYGCNFQKMY
DWIKSYDQTR LVHYEGDVEA QTVDVYSRMY PEISWIVDFA TKEEKWEKPL ILCEFVHAMG
NGPGAIKEYM DAFYKYPRLQ GGFVWEWANH GLKTKAATGE EFYGYGGDFG DTPNDGNFVM
DGLLFSDHTP TPGLVEYKKA IEPVQVIGGS YNEVEVINRY DFATLDHLQC KWSIVGDRYE
ELGGEISIPE GIQPGQTTKL AIPFTAIDSV PAGAVLQVTF TLKEATLWAE AGHEIAWGQI
ELKPTASLQS LTPPSSTCPT LTQKLPTLLS ISSATSAWEF NFVTGSLSSW KRGKSEIIHT
APVMDFYRPQ TDNDSPHDGE EWKEKHLDQT KEHTRQVSWE TSGTNVTVTV QKRIAPPVLE
WSVDTTTTYT FGETSVGIKV TGTTQGANLP KTWARIGLTM SLNSEVNGVE WFGRGPGESY
SDKKLSQRIG TWKSPVDSLF TNYEYPQESG NRTDVRWVAF QDGTGKPLLK ASFGESEGCS
FSASHYAAAD IDRATHPYLL ERERREEVLV RLDWRHHGLG TGSCGPKTME EYALKSGPFE
FSLLLE
//
