GenomeNet

Database: UniProt
Entry: BGALB_ASPNC
LinkDB: BGALB_ASPNC
Original site: BGALB_ASPNC 
ID   BGALB_ASPNC             Reviewed;        1017 AA.
AC   A2QA64;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   16-JAN-2019, entry version 70.
DE   RecName: Full=Probable beta-galactosidase B;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase B;
DE   Flags: Precursor;
GN   Name=lacB; ORFNames=An01g10350;
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:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK37216.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AM269980; CAK37216.1; ALT_SEQ; Genomic_DNA.
DR   ProteinModelPortal; A2QA64; -.
DR   SMR; A2QA64; -.
DR   STRING; 5061.CADANGAP00001004; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; A2QA64; -.
DR   PRIDE; A2QA64; -.
DR   EnsemblFungi; CAK37216; CAK37216; An01g10350.
DR   HOGENOM; HOG000181922; -.
DR   Proteomes; UP000006706; Chromosome 2R.
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     20       {ECO:0000255}.
FT   CHAIN        21   1017       Probable beta-galactosidase B.
FT                                /FTId=PRO_5000219426.
FT   ACT_SITE    196    196       Proton donor. {ECO:0000255}.
FT   ACT_SITE    308    308       Nucleophile. {ECO:0000255}.
FT   BINDING      90     90       Substrate. {ECO:0000250}.
FT   BINDING     135    135       Substrate. {ECO:0000250}.
FT   BINDING     136    136       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     137    137       Substrate. {ECO:0000250}.
FT   BINDING     195    195       Substrate. {ECO:0000250}.
FT   BINDING     265    265       Substrate. {ECO:0000250}.
FT   BINDING     373    373       Substrate. {ECO:0000250}.
FT   CARBOHYD     23     23       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    158    158       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    211    211       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    411    411       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    417    417       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    456    456       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    628    628       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    681    681       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    737    737       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    770    770       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    777    777       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    785    785       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    828    828       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    829    829       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    271    324       {ECO:0000250}.
SQ   SEQUENCE   1017 AA;  111810 MW;  3ACF69B3DFD08D04 CRC64;
     MTRITKLCVL LLSSIGLLAA AQNQTETGWP LHDDGLTTDV QWDHYSFKVH GERIFVFSGE
     FHYWRIPVPG LWRDILEKIK AAGFTTFAFY SSWAWHAPNN HTVDFSTGAR DITPIFELAK
     ELGMYIIVRP GPYINAEASA GGFPLWLTTG DYGTLRNNDS RYTEAWKPYF EKMTEITSRY
     QITNGHNTFC YQIENEYGDQ WLSDPSERVP NETAIAYMEL LESSARENGI LVPFTANDPN
     MNAMAWSRDW SNAGGNVDVV GLDSYPSCWT CDVSQCTSTN GEYVAYQVVE YYDYFLDFSP
     TMPSFMPEFQ GGSYNPWAGP EGGCGDDTGV DFVNLFYRWN IAQRVTAMSL YMLYGGTNWG
     AIAAPVTATS YDYSSPISED RSISSKYYET KLLSLFTRSA RDLTMTDLIG NGTQYTNNTA
     VKAYELRNPT TNAGFYVTLH EDSTVGTNEA FSLRVNTSAG NLIVPRLGGS IRLNGHQSKI
     IVTDFTFGSE TLLYSTAEVL TYAVIDKKPT LVLWVPTDES GEFAVKGAKS GSVVSKCQSC
     PAINFHQQGG NLIVGFTQSQ GMSVVQIDND IRVVLLDRTA AYKFWAPALT EDPLVPEDEA
     VVLIQGPYLV RSASLEKSTL AIKGDSINET AVEIFAPENV KTITWNGKQL KTSKSSYGSL
     KATIAAPASI QLPAFTSWKV NDSLPERLPT YDASGPAWVD ANHMTTANPS KPATLPVLYA
     DEYGFHNGVR LWRGYFNGTA SGVFLNVQGG SAFGFSAYLN GHFLGSYLGN ASIEQANQTF
     LFPNNITHPT TQNTLLVIHD DTGHDETTGA LNPRGILEAR LLPSDTTNNS TSPEFTHWRI
     AGTAGGESNL DPVRGAWNED GLYAERVGWH LPGFDDSTWS SVSSSSSLSF TGATVKFFRT
     TIPLDIPRGL DVSISFVLGT PDNAPNAYRA QLFVNGYQYG RFNPYIGNQV VFPVPVGVLD
     YTGENTIGVA VWAQTEDGAG ITVDWKVNYV ADSSLDVSGL ETGELRPGWS AERLKFA
//
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