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Database: UniProt
Entry: S7Z5H6_PENO1
LinkDB: S7Z5H6_PENO1
Original site: S7Z5H6_PENO1 
ID   S7Z5H6_PENO1            Unreviewed;      1011 AA.
AC   S7Z5H6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   28-FEB-2018, entry version 20.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PDE_00282 {ECO:0000313|EMBL:EPS25349.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium
OS   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.,
RA   Wang S., 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: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC       {ECO:0000256|RuleBase:RU000675, ECO:0000256|SAAS:SAAS00108875}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; KB644408; EPS25349.1; -; Genomic_DNA.
DR   EnsemblFungi; EPS25349; EPS25349; PDE_00282.
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; -; 1.
DR   Gene3D; 2.60.120.260; -; 3.
DR   Gene3D; 2.60.390.10; -; 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; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000019376};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1011       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004559715.
FT   DOMAIN      396    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                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
//
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