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Database: UniProt
Entry: K9GEM7_PEND2
LinkDB: K9GEM7_PEND2
Original site: K9GEM7_PEND2 
ID   K9GEM7_PEND2            Unreviewed;       863 AA.
AC   K9GEM7;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   16-JAN-2019, entry version 28.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PDIG_48630 {ECO:0000313|EMBL:EKV11731.1};
OS   Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV11731.1, ECO:0000313|Proteomes:UP000009882};
RN   [1] {ECO:0000313|Proteomes:UP000009882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX   PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA   Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA   Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome sequence of the necrotrophic fungus Penicillium digitatum, the
RT   main postharvest pathogen of citrus.";
RL   BMC Genomics 13:646-646(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675,
CC         ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EKV11731.1}.
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DR   EMBL; AKCT01000197; EKV11731.1; -; Genomic_DNA.
DR   EnsemblFungi; EKV11731; EKV11731; PDIG_48630.
DR   InParanoid; K9GEM7; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000009882; 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; -; 2.
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:UP000009882};
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:UP000009882}.
FT   DOMAIN      311    490       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   863 AA;  94845 MW;  053DF338F73AAFC1 CRC64;
     MGFTGASFYV DWSLVEGNPG HVITDGIWSL DEFFDAASQA GLYLIARPGP YINAETTAGG
     IPGWVLRQKA VIRSDDPEYL NATAEYMSTV GAIIERAQIT HGGPVIMAQP ENEFSTWPGV
     TDFPNDMNRD YMAYVEEQLL DEGINVPKIV NDNSVKGYFA PGSGQGAVDI YAIDAYPMRY
     DCANPSVWPT YRFPYDWQVT HKQQSPTTPF AIAEFQGGSG EGWGGVAQDM CGQLVNEEAV
     RVLYKNNYSF GVKIFNIYMT FGGTNWGNLG YMGGHTSYDY GAAITEERAI WREKFSEQKL
     EANFFKVSPA YLTATPHLGV NGTYGAPFSL AVTPLLGNGT RTNLYVVRHA DFTSTGSTQY
     TLTLSTSVGQ IEIPQLGGHL TLNGRDSKFH VTDYDVGGIN LIYSSAEIFT WAHGSGSTRV
     LILYGGAGET HEFSLPSNLG KPTVLEGHDL EIKLCGSAWV VQWHVTPARR IIRIADLWVY
     LLWRNEVYNY WVMELPASSP IGNYSSPSKS LVVVKAGYLI RTAELTNKQL RLTGDVNATT
     QIEIISSPAV GLNGIAFNGE VLQTSKMSNG NLWGTVKYDP PKFKIPDLSN LEWKFVDSLP
     EIHASYDDSA WTACKKTSTH NPRQLDTPSS LYSMDYGYHT GSLLYRGHFN ANGQESNVWL
     NVSGGLGFGH SVWLNNTFLG SWVGSSINSS VVHNMSLASV LSHGSPYVIT VLIDHMGQDE
     EAPGTDAIKV PRGILNYGIS GHAQSEVLWK LTGNLGGEQY QDLARGPLNE GGMYAERQGY
     HYPSPPSSKW KLSNPVTDGL SQAGVGFYAA YFQLNIPSGW DVPMSVVFNN SFQNSTEDTR
     GSNYRCQLFV NGYQFGKYSM YPA
//
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