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Database: UniProt
Entry: A2R3X5_ASPNC
LinkDB: A2R3X5_ASPNC
Original site: A2R3X5_ASPNC 
ID   A2R3X5_ASPNC            Unreviewed;      1015 AA.
AC   A2R3X5;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   16-JAN-2019, entry version 86.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=An14g05820 {ECO:0000313|EMBL:CAK42143.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK42143.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G.,
RA   Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K.,
RA   Andersen M.R., Bendtsen J.D., Benen J.A., van den Berg M.,
RA   Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M.,
RA   Danchin E.G., Debets A.J., Dekker P., van Dijck P.W., van Dijk A.,
RA   Dijkhuizen L., Driessen A.J., d'Enfert C., Geysens S., Goosen C.,
RA   Groot G.S., de Groot P.W., Guillemette T., Henrissat B., Herweijer M.,
RA   van den Hombergh J.P., van den Hondel C.A., van der Heijden R.T.,
RA   van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P.,
RA   van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J., Meulenberg R.,
RA   Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M.,
RA   Pal K., van Peij N.N., Ram A.F., Rinas U., Roubos J.A., Sagt C.M.,
RA   Schmoll M., Sun J., Ussery D., Varga J., Vervecken W.,
RA   van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory
RT   Aspergillus niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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}.
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DR   EMBL; AM270325; CAK42143.1; -; Genomic_DNA.
DR   RefSeq; XP_001401205.1; XM_001401168.1.
DR   ProteinModelPortal; A2R3X5; -.
DR   STRING; 5061.CADANGAP00011297; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; A2R3X5; -.
DR   EnsemblFungi; CAK42143; CAK42143; An14g05820.
DR   GeneID; 4987440; -.
DR   KEGG; ang:ANI_1_1530124; -.
DR   HOGENOM; HOG000181922; -.
DR   Proteomes; UP000006706; Chromosome 1R.
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:UP000006706};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888, ECO:0000313|EMBL:CAK42143.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869, ECO:0000313|EMBL:CAK42143.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1015       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002645633.
FT   DOMAIN      392    570       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1015 AA;  112041 MW;  EB242EAE241266E2 CRC64;
     MKTSFLLAIG LAVEACLGLV SAPNYVRQIN ATDSSLQDIV TWDEYSIRVR GERILLLLGE
     FHPFRLPCPG LWLDVFQKVR ALGFSAVSFY VDWALLEGER GSIRADGVFA LEEFFQAATE
     AGLYLTARPG PYINAEVSGG GFPGWLKRVQ GRLKTTDQGY LDAITPYMQA IGRIIAKAQI
     TNGGPVILFQ PENEYTACVQ DEGYTQKEYM AYVEEQYRKA GIVVPFIVND ADPMGNFAPG
     TGVGAVDIYS FDDYPLQWST APSNPSNWSS LISPLLSYNE TVHEEQSPTT PFSISEFQGG
     VPDAWGGVGI ETSAAYIGPE FERIFYKINY GFRAAIQNLY MIFGGTNWGN LGHSGGYTSY
     DVGAAIAEDR QVIREKYSEL KLQSNFLQAS SAYLETHSDN GSYGIYTDAT SLAVTRLAGN
     PTNFYVVRHG ELTSRESTSY KLRVNTSAGN LAIPQLSGSL SLHGRDSKIH LVDYNVGNVS
     LIYSTAELFT WKQAGSKSVV VLYGGEDELH EFAVPANKGK PTSIEGDGLQ VQQINSTTVI
     QWAVQPSRRV VHFSDTLEVH LLWRNEAYNY WVLDLPVPGA IGRHVSRSHT NRSVIVKAGY
     LLRTAEIIGT SLYLTGDINT TTTIELISAP QPVTSILFNK NRIPTTITSP GRLTGTLTYH
     KPNISLPDLT TLDWYYLNTL PEVHDPTYDD HLWTPCTHTT TANPRNLTTP TSLYASDYGY
     NGGTLLYRGT FTATGNETSL YLLTEGGYAY GHSIWLNNTF LASWPGNPAF LLSNQTITFP
     SPLTPGTTYK LTILIDHLGN DENFPANGEF MKDPRGILDY TLHGRDDKSA ISWKMTGNFG
     GESYADLSRG PLNEGALFAE RKGYHLPGAP TEQWTKRSPF DGLPEDERPG VGFFATKFDL
     QIPDGYDVPI SVVFENSTMA GDGSGPARFR SELFVNGWQF GKYVNHIGPQ LSYPVPEGIL
     NYNGSNYLAL TIWAMDEKSF KLDGLRLQAN AVVQSGYRKP SLVKGEVYKE RVDSY
//
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