ID S7ZKF7_PENO1 Unreviewed; 1035 AA.
AC S7ZKF7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, 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=PDE_04120 {ECO:0000313|EMBL:EPS29171.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS29171.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS29171.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB644411; EPS29171.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZKF7; -.
DR SMR; S7ZKF7; -.
DR STRING; 933388.S7ZKF7; -.
DR eggNOG; KOG2024; Eukaryota.
DR HOGENOM; CLU_002346_0_0_1; -.
DR OrthoDB; 276651at2759; -.
DR PhylomeDB; S7ZKF7; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000019376; 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:UP000019376}.
FT DOMAIN 737..1028
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1035 AA; 116953 MW; 8C406F35A977E4B5 CRC64;
MSFPKAQPDW NNLGVLHRNT LPSRAHFYTY GSEDKALTFN REESEYISLN GTWKFRHDTS
PFEAPEWSSV NPLTWDDIKV PGMWQVQGYS HPTYTNVNYP FHVDPPNVPI LNETGSYWRQ
FVTPTSWDGQ QIRIRFEGVD SAFHLWVNGE EVGYSQGSRN PSEFDITSLL RPAGTVNTLA
VRVYEFCDGS YIERQDQWLL SGIFRDVGLL GFPKSSIVDF DAVPTLSEDL VSGELITKVK
IQGETGDVKV KLLRPDGSLL EQSSFLSSES SKIKVTGDEL KLWSAEHPVL YTLLVTFNGR
TIPQRIGFRR IERKGANFHV NGRPIMLYGM NRHEHHHLFG RAVPYESMRA DLVMMKKYNI
NALRCSHQPN DPRLYEVCDE LGLYVIAEAD LETHGFDPVE RSNIPDQHLM TEYEIQEASY
KRATKWTSDN PEWKEAYLDR AEQLVQRFKN YSCIIFWSLG NEAFYGQNHA SMYKWIKEAD
PTRLVHYEGD RDAISADMYS TMYWSPEALK QHVADKPDKA MIQCEYAHAM GNGPGGLKEY
IDTYRSEPLL QGGFIWEWCN HGMLKREGTQ SYYAYGGDFG DKPNDADFIL DGMVYSDHTP
TPGLIEYKKA IEPVTIASKE GRLEVTNHYD FSTLDHLSAS WHIVKEAGNT EPVAWQLPEI
KPGETKVVDL PEGVTFGSEP SWFAANFSLK DATSWAPQGH EIAWAQIPLF DESKVTLPLV
KSPSSKLSIT ENQGKLYIYS DSFAANFTYD LVRGNLAWST DSGKVFHSGP QLGFYRALTQ
NDVGAGGPLA EWKRFRVDSL CRMLVQGSTW SNNDDGSISI TTKVRVAPVV LEWAMVANLT
YTITGSSVQL HVKGDFTGTF PQVIPRIGLT VRLPRRYEAA TWFGRGPGES YRDKKAAARF
GTYTSSIDTG LETPYEWPQE NGNRTDTRWV RVHAASDETA YAASAKAQPS LPQIEARMDS
PFNFSLSRYS IEELDRAKHP HELSALENET EFTIDFAHHG IGTGSCGPGA FEGNRLEAGP
FEFTTVFRLL SGKSE
//
