ID   BGALC_NEOFI             Reviewed;         983 AA.
AC   A1DM65;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 88.
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=NFIA_052310;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
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; DS027698; EAW15886.1; -; Genomic_DNA.
DR   RefSeq; XP_001257783.1; XM_001257782.1.
DR   AlphaFoldDB; A1DM65; -.
DR   SMR; A1DM65; -.
DR   STRING; 331117.A1DM65; -.
DR   GlyCosmos; A1DM65; 11 sites, No reported glycans.
DR   EnsemblFungi; EAW15886; EAW15886; NFIA_052310.
DR   GeneID; 4584298; -.
DR   KEGG; nfi:NFIA_052310; -.
DR   VEuPathDB; FungiDB:NFIA_052310; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_005732_2_1_1; -.
DR   OMA; PEFEGGW; -.
DR   OrthoDB; 1032627at2759; -.
DR   Proteomes; UP000006702; 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; Beta-galactosidase, domain 2; 1.
DR   Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 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:SF125; BETA-GALACTOSIDASE C-RELATED; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF13364; BetaGal_ABD2; 2.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..983
FT                   /note="Probable beta-galactosidase C"
FT                   /id="PRO_0000395239"
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        804
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        257..304
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   983 AA;  107868 MW;  DE259315212C11F0 CRC64;
     MRIFSFLFLL LLGILTGQGL VSGTDNGKTT DVTWDKYSLS VKGQRLFVFS GEFHYQRLPV
     PELWLDVFQK LRANGFNAIS VYFFWSFHSA SEGEFDFENG AHDIQRLFDY AKEAGLYVIA
     RAGPYCNAET SAGGFALWAA NGQMGNERTS DEAYYEKWRP WILEVGKIIA KNQITNGGPV
     ILNQHENELT ETTYDPNHTL VVYMKQIAQV FEEAGIVVPS SHNEKGMRGV SWSTDYHNVG
     GAVNIYGLDS YPGGLSCTNP NSGFRLVRTY YQWFQNYSST QPSYMPEFEG GWFQPWGGSF
     YDTCATELSP EFPDVYYKNN IGSRVTLHSI YMTYGGTNWG HSAAPVVYTS YDYAAPLRET
     REIRDKLKQT KLIGLFTRVS TDLLKTYMEG NGTGYTSDSS IYTWSLRNPD TNAGFYVLAH
     STSSARDVTT FSLNATTSAG AISIPDIELN GRQSKIIVTD YNFGTNSTLL FSSAEVLTYA
     NLDVNVLVFY LNVGQKGTFA LKDEPKLAFQ TYGNSNVTTS ESSYGTQYSY TQGEGVTAVK
     FSNGVLAYLL DKESAWNFFA PPTTSSPQVA PNEHILVQGP YLVRGASINH GTVEITGDNA
     NTTSIEVYTG NSQVKKVKWN GKTIETRKTA YGSLIGTVPG AEDVKIRLPS LDSWKAQDTL
     PEIQPDYDDS TWTVCNKTTS VNAIAPLSLP VLYSGDYGYH AGTKVYRGRF DGRNVTGANV
     TVQNGAAAGW AAWVNGQYAG GSAGSPSLAA TSAVLTFNGL SLKDRDNVLT VVTDYTGHDQ
     NSVRPKGTQN PRGILGATLT GGGNFTSWRI QGNAGGEKNI DPVRGPMNEG GLYGERMGWH
     LPGYKVPKSA SKSSPLDGVS GAEGRFYTTT FKLKLDKDLD VPIGLQLGAP EGTKAVVQVF
     MNGYQFGHYL PHTGPQSLFP FPPGVINNRG ENTLAISMWA LTDAGAKLDK VELVAYGKYR
     SGFDFNQDWG YLQPGWKDRS QYA
//