GenomeNet

Database: UniProt
Entry: BGALC_ASPNC
LinkDB: BGALC_ASPNC
Original site: BGALC_ASPNC 
ID   BGALC_ASPNC             Reviewed;         994 AA.
AC   A2QL84;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   07-NOV-2018, entry version 68.
DE   RecName: Full=Probable beta-galactosidase C;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase C;
DE   Flags: Precursor;
GN   Name=lacC; ORFNames=An06g00290;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
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.E., van den Berg M.,
RA   Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M.,
RA   Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M.,
RA   van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S.,
RA   Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T.,
RA   Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M.,
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.E.C.,
RA   Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G.,
RA   Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U.,
RA   Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B.,
RA   Zeng A.-P., van Ooyen A.J.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   -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
DR   EMBL; AM270108; CAK44945.1; -; Genomic_DNA.
DR   ProteinModelPortal; A2QL84; -.
DR   SMR; A2QL84; -.
DR   STRING; 5061.CADANGAP00004935; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; A2QL84; -.
DR   EnsemblFungi; CAK44945; CAK44945; An06g00290.
DR   HOGENOM; HOG000181922; -.
DR   OrthoDB; EOG092C0SLI; -.
DR   Proteomes; UP000006706; Chromosome 8ER.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    994       Probable beta-galactosidase C.
FT                                /FTId=PRO_5000220037.
FT   ACT_SITE    184    184       Proton donor. {ECO:0000255}.
FT   ACT_SITE    283    283       Nucleophile. {ECO:0000255}.
FT   BINDING      78     78       Substrate. {ECO:0000250}.
FT   BINDING     123    123       Substrate. {ECO:0000250}.
FT   BINDING     124    124       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     125    125       Substrate. {ECO:0000250}.
FT   BINDING     183    183       Substrate. {ECO:0000250}.
FT   BINDING     247    247       Substrate. {ECO:0000250}.
FT   BINDING     350    350       Substrate. {ECO:0000250}.
FT   CARBOHYD     88     88       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    272    272       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    388    388       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    407    407       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    433    433       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    500    500       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    514    514       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    521    521       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    584    584       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    600    600       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    674    674       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    712    712       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    717    717       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    757    757       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    861    861       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    969    969       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    253    301       {ECO:0000250}.
SQ   SEQUENCE   994 AA;  108643 MW;  1B20B22277763D58 CRC64;
     MKLQSILSCW AILVAQIWAT TDGLTDLVAW DPYSLTVNGN RLFVYSGEFH YPRLPVPEMW
     LDVFQKMRAH GFNAVSLYFF WDYHSPINGT YDFETGAHNI QRLFDYAQEA GIYIIARAGP
     YCNAEFNGGG LALYLSDGSG GELRTSDATY HQAWTPWIER IGKIIADNSI TNGGPVILNQ
     IENELQETTH SASNTLVEYM EQIEEAFRAA GVDVPFTSNE KGQRSRSWST DYEDVGGAVN
     VYGLDSYPGG LSCTNPSTGF SVLRNYYQWF QNTSYTQPEY LPEFEGGWFS AWGADSFYDQ
     CTSELSPQFA DVYYKNNIGQ RVTLQNLYML YGGTNWGHLA APVVYTSYDY SAPLRETRQI
     RDKLSQTKLV GLFTRVSSGL LGVEMEGNGT SYTSTTSAYT WVLRNPNTTA GFYVVQQDTT
     SSQTDITFSL NVNTSAGAFT LPNINLQGRQ SKVISTDYPL GHSTLLYVST DIATYGTFGD
     TDVVVLYARS GQVVSFAFKN TTKLTFEEYG DSVNLTSSSG NRTITSYTYT QGSGTSVVKF
     SNGAIFYLVE TETAFRFWAP PTTTDPYVTA EQQIFVLGPY LVRNVSISGS VVDLVGDNDN
     ATTVEVFAGS PAKAVKWNGK EITVTKTDYG SLVGSIGGAD SSSITIPSLT GWKVRDSLPE
     IQSSYDDSKW TVCNKTTTLS PVDPLSLPVL FASDYGYYTG IKIYRGRFDG TNVTGANLTA
     QGGLAFGWNV WLNGDLVASL PGDADETSSN AAIDFSNHTL KQTDNLLTVV IDYTGHDETS
     TGDGVENPRG LLGATLNGGS FTSWKIQGNA GGAAGAYELD PVRAPMNEGG LLAERQGWHL
     PGYKAKSSDG WTDGSPLDGL NKSGVAFYLT TFTLDLPKKY DVPLGIQFTS PSTVDPVRIQ
     LFINGYQYGK YVPYLGPQTT FPIPPGIINN RDKNTIGLSL WAQTDAGAKL ENIELISYGA
     YESGFDAGNG TGFDLNGAKL GYQPEWTEAR AKYT
//
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