ID S7Z5H6_PENO1 Unreviewed; 1011 AA.
AC S7Z5H6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN ORFNames=PDE_00282 {ECO:0000313|EMBL:EPS25349.1};
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:EPS25349.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS25349.1, 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 ECO:0000256|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; KB644408; EPS25349.1; -; Genomic_DNA.
DR AlphaFoldDB; S7Z5H6; -.
DR SMR; S7Z5H6; -.
DR STRING; 933388.S7Z5H6; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OrthoDB; 1032627at2759; -.
DR PhylomeDB; S7Z5H6; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR018954; Betagal_dom2.
DR InterPro; IPR037110; Betagal_dom2_sf.
DR InterPro; IPR025972; BetaGal_dom3.
DR InterPro; IPR036833; BetaGal_dom3_sf.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF122; BETA-GALACTOSIDASE A-RELATED; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1011
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004559715"
FT DOMAIN 396..576
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1011 AA; 110500 MW; 50D645E766B5BB77 CRC64;
MKLLSSLALA ALAAQVSGAA ISHKLDGFTL REHADASKRE LLQKYVTWDK HSIFINGERL
MMFSGEVHPY RLPVASLYID VFEKIKALGF NCVSFYVDWA LLEGKPGHYT AEGIFDLQPF
FDAAKEAGIY LLARPGPYIN AEVSGGGFPG WLQRVNGTLR TSIGDYLKST DNYASHIAKT
IAKAQITNGG PIILYQPENE YSGACCGYED FPDGSYMQYI EDHARDAGIV VPFISNDAYA
GGHNAPGTGK GAVDIYGHDG YPLGFDCANP SVWPDGNLPT NYHTLHEEQS PTTPFSIVEF
QGGAFDPWGG VGFAKCAHLL NHEFERVFYK NDFSFGVTFF NLYMIFGGTN WGNLGHPGGY
TSYDYGSAIS ESRNVTREKY SELKLLGNFA KVSPGYVVAN PGNLTTSKYT KTADLTVTPL
LGESSSAGSF FVIRHSNYNS QASVKYQLTL PTSAGELTIP QLGGELTLSG RDSKIHVTDY
DVAGSNILYS TAEVFTWKKF DNGKVLILYG GPGEHHEFAV TGASASSVIE GSSSGITSKK
IGDALVVAWD VSSKRRIIKI GDLKVFLLDR NSAYNYWVPH LPTKGKAPGY VSKKAIDSSI
IVKAGYLVRS AFLSGKDLHI QADFNATTPI EIIGAPSSAK NLIINGKKTK TNVDDNGIWS
ASVSYSTPEI HLPSLKDLKW QSIDTLPEVK NSYDDSAWTS ADQPHTLNTA HELQTPTTLF
SSDYGYHTGT LLYRGHFVAN GKESIFFIQT QGGSAYGHSV WVNETYVGSW EGSGSNDNYN
ATYTLPSLAT GKKYVITVVI DNMGLDENWV IGQEGMKNPR GIIRYNLAGH DASAISWKLT
GNLGGEDYRD TVRGPLNEGG LYAERQGFHQ PKPSTKNWDS SSPFTGLTKP GIRFYSASFD
LDLPSGYDIP LYFNFGNSTA PPDAYRVQLF VNGYQYGKYV NNVGPQTSFP VPEGILNYHG
TNWIALSLWA QQESGAKLNS FELINTTPVL TSLDKVKSVD QPKYKSRKGA Y
//
