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Database: UniProt
Entry: A0A100IK03_ASPNG
LinkDB: A0A100IK03_ASPNG
Original site: A0A100IK03_ASPNG 
ID   A0A100IK03_ASPNG        Unreviewed;      1029 AA.
AC   A0A100IK03;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   16-JAN-2019, entry version 15.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=ABL_05321 {ECO:0000313|EMBL:GAQ42660.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ42660.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ42660.1}.
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DR   EMBL; BCMY01000008; GAQ42660.1; -; Genomic_DNA.
DR   EnsemblFungi; GAQ42660; GAQ42660; ABL_05321.
DR   Proteomes; UP000068243; 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:UP000068243};
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:UP000068243};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19   1029       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007087481.
FT   DOMAIN      408    585       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1029 AA;  113439 MW;  8B3CA1BB16F4493B CRC64;
     MKASFLLSVG LAAKACLGLV TAPKYVRQEN TTASSLQDIV TWDEYSIRVH GERVLLLSGE
     FHPFRLPSPG LWLDVFQKVR ALGFSAVSFY VDWALLEGER GSIRADGVFA LEEFFQAATE
     AGLYLTARPG PYINAEVSGG GFPGWLERVQ GRLKTTDQGY LDAITPYMQA IGRIIAKAQI
     TNGGPVILFQ PENEYTACVQ DVGYTQINNY SMPDYNSSCL QKDYMAYVED QYRKAGIVVP
     FIVNDAEPMG NFAPGTGVGA VDIYSFDDYP MHWSTAPSNP SNWSSVVNPL LSYNETVHEK
     QSPTTPFSIS EFQGGVPDGW GGVGVDTSAA YIGPEFARIF YKINYGFRTA IQNLYMIFGG
     TNWGNLGHPG GYTSYDVGAA IAEDREVIRE KYSELKLQSN FLQASPAYLE SHPENGSYGI
     YADTTSLAVT RLAGNPTNFY VVRHGELTSQ ESTSYKLRVN TTAGSLTIPQ LGGTLSLNGR
     DSKIHLVDYN VGNVNLIYSS AELFTWKQTG SKSVVVLYGG EDELHEFAVP VNIGKPTFIE
     GDDLQIQQIN STTVIQWAVQ PSRRVVHFGN TLEVHLLWRN EAYNYWVLDL PVPGAIGRHV
     SQSHANRSVI VKAGYLLRTA ELTGTALYLT GDINTTTTLE LISAPQPVTS IFFNNQSVQT
     SVTSGRLTGT LTYQKPNISL TDLTTLDWHY LDTLPEVRDS TYNDDLWTPC THTTTANPRN
     LTTPTSLYAS DYGYNGGSLL YRGTFTATGN ETSLYLLTEG GYAYGYSIWL NNTFLTSWLG
     DPLYMFSNQT VTIPSSLTPE TTYTLTILID HLGNDENFPA NGEFMKDPRG ILDYTLHGRD
     DKSAISWKLT GNFGGEHYAD LTRGPLNEGA FFAERKGYHL PGAPVEKWTK RSPFEGLPED
     EAPGVGFFAT TFDLNVPDGY DVPIGVVFEN STTVGDGSEP ARFRSELFVN GWQFGKYVNH
     IGPQSSFPVP EGILNYNGSN YLALTIWAMD ENSFKLDGLR LQANAVVQSG YRKPSLVDGE
     VYKERAGSY
//
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