ID   BGALC_ASPFU             Reviewed;         983 AA.
AC   Q4WNE4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 101.
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=AFUA_6G06660;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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; AAHF01000006; EAL88520.1; -; Genomic_DNA.
DR   RefSeq; XP_750558.1; XM_745465.1.
DR   AlphaFoldDB; Q4WNE4; -.
DR   SMR; Q4WNE4; -.
DR   STRING; 330879.Q4WNE4; -.
DR   GlyCosmos; Q4WNE4; 12 sites, No reported glycans.
DR   EnsemblFungi; EAL88520; EAL88520; AFUA_6G06660.
DR   GeneID; 3508765; -.
DR   KEGG; afm:AFUA_6G06660; -.
DR   VEuPathDB; FungiDB:Afu6g06660; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_005732_2_1_1; -.
DR   InParanoid; Q4WNE4; -.
DR   OMA; PEFEGGW; -.
DR   OrthoDB; 1032627at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
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_0000395237"
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
//