GenomeNet

Database: UniProt
Entry: BGALC_NEOFI
LinkDB: BGALC_NEOFI
Original site: 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   16-JAN-2019, entry version 73.
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
OS   A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
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.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   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.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
DR   EMBL; DS027698; EAW15886.1; -; Genomic_DNA.
DR   RefSeq; XP_001257783.1; XM_001257782.1.
DR   ProteinModelPortal; A1DM65; -.
DR   SMR; A1DM65; -.
DR   STRING; 36630.CADNFIAP00004465; -.
DR   PRIDE; A1DM65; -.
DR   EnsemblFungi; EAW15886; EAW15886; NFIA_052310.
DR   GeneID; 4584298; -.
DR   KEGG; nfi:NFIA_052310; -.
DR   EuPathDB; FungiDB:NFIA_052310; -.
DR   HOGENOM; HOG000181922; -.
DR   OMA; EFEGGWF; -.
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; 2.60.120.260; -; 2.
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; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    983       Probable beta-galactosidase C.
FT                                /FTId=PRO_0000395239.
FT   ACT_SITE    188    188       Proton donor. {ECO:0000255}.
FT   ACT_SITE    287    287       Nucleophile. {ECO:0000255}.
FT   BINDING      82     82       Substrate. {ECO:0000250}.
FT   BINDING     127    127       Substrate. {ECO:0000250}.
FT   BINDING     128    128       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     129    129       Substrate. {ECO:0000250}.
FT   BINDING     187    187       Substrate. {ECO:0000250}.
FT   BINDING     251    251       Substrate. {ECO:0000250}.
FT   BINDING     353    353       Substrate. {ECO:0000250}.
FT   CARBOHYD    197    197       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    276    276       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    391    391       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    434    434       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    466    466       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    516    516       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    601    601       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    676    676       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    714    714       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    719    719       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    804    804       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    257    304       {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
//
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