BGALC_NEOFI
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 03-AUG-2022, entry version 85.
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 / NRRL 181
RC / 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; 36630.CADNFIAP00004465; -.
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; 179316at2759; -.
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; -; 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..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
