BGALC_PENRW
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 03-AUG-2022, entry version 72.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM920429; CAP74292.1; -; Genomic_DNA.
DR RefSeq; XP_002560145.1; XM_002560099.1.
DR AlphaFoldDB; B6H5X9; -.
DR SMR; B6H5X9; -.
DR STRING; 1108849.XP_002560145.1; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR EnsemblFungi; CAP74292; CAP74292; PCH_Pc14g01510.
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; 179316at2759; -.
DR BioCyc; PCHR:PC14G01510-MON; -.
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; -; 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..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
