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 03-AUG-2022, entry version 80.
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;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., 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., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT 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. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK37216.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM269980; CAK37216.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A2QA64; -.
DR SMR; A2QA64; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; A2QA64; -.
DR EnsemblFungi; CAK37216; CAK37216; An01g10350.
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; 2.60.390.10; -; 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; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1017
FT /note="Probable beta-galactosidase B"
FT /id="PRO_5000219426"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 271..324
FT /evidence="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