ID   BGALC_ASPOR             Reviewed;         984 AA.
AC   Q2UMD5;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 94.
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=AO090003000042;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007155; BAE57280.1; -; Genomic_DNA.
DR   RefSeq; XP_001819282.1; XM_001819230.1.
DR   AlphaFoldDB; Q2UMD5; -.
DR   SMR; Q2UMD5; -.
DR   STRING; 510516.Q2UMD5; -.
DR   Allergome; 1261; Asp o Lactase.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; Q2UMD5; 12 sites, No reported glycans.
DR   EnsemblFungi; BAE57280; BAE57280; AO090003000042.
DR   GeneID; 5991265; -.
DR   KEGG; aor:AO090003000042; -.
DR   VEuPathDB; FungiDB:AO090003000042; -.
DR   HOGENOM; CLU_005732_2_1_1; -.
DR   OMA; PEFEGGW; -.
DR   OrthoDB; 1032627at2759; -.
DR   Proteomes; UP000006564; Chromosome 2.
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..984
FT                   /note="Probable beta-galactosidase C"
FT                   /id="PRO_0000395238"
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        421
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        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        602
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        677
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        715
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        720
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        759
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        805
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        257..304
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   984 AA;  108653 MW;  8326D1E294ACDECE CRC64;
     MRLLSFIYLV WLALLTGTPQ VSATDNGKTS DVAWDKYSLS VKGERLFVFS GEFHYQRLPV
     PELWLDVFQK LRANGFNTIS VYFFWSYHSA SEDVFDFTTG AHDIQRLFDY AKQAGLYVIA
     RAGPYCNAET SAGGFALWAA NGQMGSERTS DEAYYKKWKP WILEVGKIIA ANQITNGGPV
     ILNQHENELQ ETTYDSNDTK VIYMEQVAKA FEEAGVVVPS SHNEKGMRTV SWSTDYKNVG
     GAVNVYGLDS YPGSLSCANP NSGFNLLRTY YQWFQNYSYT QPEYLAEFEG GWFQPWGGSF
     YDSCASELSP EFADVYYKNN IGSRVTLHNI YMTFGGTNWG HSAAPVVYTS YDYGSPLRET
     REIRDKLKQT KLLGLFTRVS KDLLKTYMEG NGTSYTSDDS IYTWALRNPD SDAGFYVVAH
     NTSSSREVTT FSLNITTSAG AMTIPDIELD GRQSKIIVTD YSIGSESSLL YSSAEVLTYA
     TLDVDVLVFY LNAGQKGAFV FKDAPADLKY QTYGNSNLSA LETSQGTQYS YTQGEGVTAV
     KFSNGVLVYL LDKETAWNFF APPTVSSPTV APNEHILVFG PYLVRGASIK HDTVEIVGDN
     SNSTSIEIYT GDEHVKKVSW NGNLIDTRAT AYGSLIGTVP GAEDIEISLP SLSSWKAQDT
     LPEISPDYDD SRWTICNKTT SVNSVAPLSL PVLYSGDYGY HTGTKIYRGR FDGQNATGAN
     VTVQNGVAAG WAAWLNGAYV GGFSGDPDKV ASWEVLKFNH SSLRSRDNVL TIITDYTGHD
     QNSQKPIGTQ NPRGIMGATL IGGGNFTLWR IQGNAGGEKN IDPVRGPMNE GGLYGERMGW
     HLPGYQVPES ALDSSPLEGV SGAEGRFYTT SFQLDLEEDL DVPIGLQLSA PAGTEAVVQI
     FMNGYQFGHY LPHIGPQSLF PFPPGVIKNR GQNSLAISMW ALTDAGARLE QVELKAYAKY
     RSGFDFNRDW TYLQPGWKDR TEYA
//