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 03-AUG-2022, entry version 80.
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;
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}.
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DR EMBL; AM270108; CAK44945.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QL84; -.
DR SMR; A2QL84; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; A2QL84; -.
DR EnsemblFungi; CAK44945; CAK44945; An06g00290.
DR VEuPathDB; FungiDB:An06g00290; -.
DR HOGENOM; CLU_005732_2_1_1; -.
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; 2.60.390.10; -; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..994
FT /note="Probable beta-galactosidase C"
FT /id="PRO_5000220037"
FT ACT_SITE 184
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 861
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 969
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 253..301
FT /evidence="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
