ID   BGALC_PENRW             Reviewed;         982 AA.
AC   B6H5X9;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 77.
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=Pc14g01510;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(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; AM920429; CAP74292.1; -; Genomic_DNA.
DR   RefSeq; XP_002560145.1; XM_002560099.1.
DR   AlphaFoldDB; B6H5X9; -.
DR   SMR; B6H5X9; -.
DR   STRING; 500485.B6H5X9; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; B6H5X9; 7 sites, No reported glycans.
DR   GeneID; 8314314; -.
DR   KEGG; pcs:Pc14g01510; -.
DR   VEuPathDB; FungiDB:PCH_Pc14g01510; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_005732_2_1_1; -.
DR   OMA; PEFEGGW; -.
DR   OrthoDB; 1032627at2759; -.
DR   BioCyc; PCHR:PC14G01510-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c14.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..982
FT                   /note="Probable beta-galactosidase C"
FT                   /id="PRO_5000409114"
FT   ACT_SITE        186
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        285
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        389
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        600
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        675
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        718
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        785
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        255..302
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   982 AA;  107330 MW;  CB71A29036AA41A1 CRC64;
     MRLFALLPVL LGLISSHFVS ATDNGKTTDV TWDKYSLSVK GERVYVFSGE FHYQRLPVPE
     LWLDVFQKLR ANGFNAISIY FFWSFHSASE DTFDFENGAH DVQRVFDYAK QAGLYVIARA
     GPYCNAETSA GGFALWASNG QMGSTRTSAS SYYDRWYPWI QEIGKIIAAN QITNGGPVIL
     NQHENELQET IHSADNTVVK YMEQIKAAFS DAGIIVPSTH NEKGMRSMSW STDYQDVGGA
     VNIYGLDSYP GGLSCTNPNS GFNLVRTYYQ WFQNYSSSQP EYLPEFEGGW FSAWGGSFYD
     QCSTELSPEF ADVYYKNNIG SRVTLHNIYM VMGATSWGQS AAPVVYTSYD YSAPMRETRE
     IRDKLKQTKL IGLFTRVSSG LLQTQMEGNG TGYTSDASIY TWALRNPETH AGFYVLAHST
     SSSRAVTTTS LNVNTSAGAL TIPNIELAGR QSKIIVTDYQ TGDGSSLLYS SAEVLTYATL
     DVDVIVFYLN IGQKGEFAFK DAPTHLTFKT YGNSKVSSAK SDHGTKYTYC QGDGTTVLKF
     SHGVLVYLLD KETAWNFFAV PTTSNPRVAP SEQILALGPY LVRTASVSGH TVSLVGDNAN
     ATSLEVYTGN SKVTQIKWNG KETPTKKTAY GSLIGSAPGA EHAKLSLPTL KSWKAQDTLP
     EINPDYDDSR WTVCNKTTSV NSVAPLTLPV LYSGDYGYHA GTKIYRGRFD GVTATGANIT
     VQNGVAAGWA AWLNGVYVGG AIGDPDLAAT SAELEFTSST LRRKDNVLTV VMDYTGHDQA
     NVKPNGSQNP RGILGATLLG GDFTSWRIQG NAGGEANIDP VRGPMNEGGL YGERLGWHLP
     GYKGSKTATS ESPLDGVSGA AGRFYTTTFK LDLDSDLDVP IGLQLGASAD APAVVQIFMN
     GYQFGHYLPH IGPQTRFPFP PGVINNRGEN TLAISLWALT EQGARLSQVD LVAYGAYRTG
     FNFNHDWSYL QPQWENNRGQ YV
//