BGALC_ASPFC
ID BGALC_ASPFC Reviewed; 983 AA.
AC B0Y752;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=AFUB_072590;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499599; EDP49233.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y752; -.
DR SMR; B0Y752; -.
DR EnsemblFungi; EDP49233; EDP49233; AFUB_072590.
DR VEuPathDB; FungiDB:AFUB_072590; -.
DR HOGENOM; CLU_005732_2_1_1; -.
DR PhylomeDB; B0Y752; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
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; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..983
FT /note="Probable beta-galactosidase C"
FT /id="PRO_0000395235"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 287
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 257..304
FT /evidence="ECO:0000250"
SQ SEQUENCE 983 AA; 108035 MW; 61D896C6685A50A5 CRC64;
MRIFSFLFLL LLGILTGQGL VSGTDNGKTT DVTWDKYSLS VKGQRLFVFS GEFHYQRLPV
PELWLDVFQK LRANGFNAIS VYFFWSFHSA SEGEFDFENG AHDIQRLFDY AKEAGLYVIA
RAGPYCNAET SAGGFALWAA NGQMGNERTS DEAYYEKWRP WILEVGKIIA KNQITNGGPV
ILNQHENELV ETTYDPNHTL VVYMKQIAQV FEEAGIVVPS SHNEKGMRGV SWSTDYHNVG
GAVNIYGLDS YPGGLSCTNP NSGFNLVRTY HQWFQNYSFT QPSYLPEFEG GWFQPWGGSF
YDTCATELSP EFPDVYYKNN IGSRVTLHSI YMTYGGTNWG HSAAPVVYTS YDYAAPLRET
REIRDKLKQT KLIGLFTRVS KDLLKTYMEG NGTGYTSDSS IYTWSLRNPD TNAGFYVLAH
STSSTRDVTT FTLNVTTSAG AISIPDIELN GRQSKIIVTD YNFGTNSTLL FSSAEVLTYA
NLDVNVLVFY LNVGQKGTFV FKDEPKLAFQ TYGNSNLTTS ESSYGTQYSY TQGKGVTAVK
FSNGVLAYFL DKESAWNFFA PPTTSSPQVA PNEHILVQGP YLVRGASVNH GTVEITGDNA
NTTSIEVYTG NSQVKKIKWN GKTIETRKTA YGSLIGTAPG AEDVKIQLPS LDSWKAQDTL
PEIQPDYDDS KWTVCNKTTS VNAIAPLSLP VLYSGDYGYH AGTKVYRGRF DGRNVTGANV
TVQNGAAAGW AAWVNGQYAG GSAGSPNLAA TSAVLTFNSS SLKDQDNVLT VVTDYTGHDQ
NSVRPKGTQN PRGILGATLI GGGNFTSWRI QGNAGGEKNI DPVRGPMNEG GLYGERMGWH
LPGYKVPKSA SKSSPLDGVS GAEGRFYTTT FKLKLDKDLD VPIGLQLGAP EGTKAVVQVF
MNGYQFGHYL PHTGPQSLFP FPPGVINNRG ENTLAISMWA LTDAGAKLDK VELVAYGKYR
SGFDFNQDWG YLQPGWKDRS QYA