BGALC_SCLS1
ID BGALC_SCLS1 Reviewed; 984 AA.
AC A7EZS5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, 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=SS1G_10842;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476636; EDN94967.1; -; Genomic_DNA.
DR RefSeq; XP_001588395.1; XM_001588345.1.
DR AlphaFoldDB; A7EZS5; -.
DR SMR; A7EZS5; -.
DR STRING; 665079.A7EZS5; -.
DR GeneID; 5484283; -.
DR KEGG; ssl:SS1G_10842; -.
DR VEuPathDB; FungiDB:sscle_09g069470; -.
DR InParanoid; A7EZS5; -.
DR OMA; PEFEGGW; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
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; -; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..984
FT /note="Probable beta-galactosidase C"
FT /id="PRO_0000395241"
FT ACT_SITE 184
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
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 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 870
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 253..300
FT /evidence="ECO:0000250"
SQ SEQUENCE 984 AA; 107521 MW; 8DD71B799E922286 CRC64;
MRLLNIFTTL CLLLWSGAAT NDGLTDVVEW DPYSLTINGD RVFIYSAEFH YQRMPVPELW
LDIFQKFRAN GFNTISVYFF WSYHEASKGS FDFETSGKNV QRVLDYAKEA GIYVIARAGP
YCNAETSAGG LALWGSDGSM GTLRTNNAAY YQSWQPWIKE IGAILAKNQV TNGGPVILNQ
VENELQETVH SATNTLVLYM EQLETAFRAA GITVPFSHNE KGQRSQSWST DYENVGGAVN
VYGLDSYPGG LSCTNSNSGF SVVRNYYQWF SNYSYTQPSY FPEFEGGYFT PWGGSFYDEC
QSELDPSFPD VYYKNNIGQR TTLMSLYMAW GGTNWGHSAA PVVYTSYDYA APLRETRQIR
DKLSQTKLIG LFTRVSTDLL KTDMIGNGTG HSVSSTGIWS WVLRNPDTQA GFTVVQQASS
GSRASVTFDV YLNTSLGAVT ASDVNLNGRQ SKILVTDYNF GNHTLLYASS DILTYGTFDV
DVLVFYLEQG QIGQFALKTT SKLTYQVYGN SVFAANSSST STSQTFTYTQ GAGQTVVQFS
DGALVYLLDQ PSAWKFWAPP TTSNPQVKPN EQIFVLGPYL VRNASISSGV AQIFGDNDNA
TTIEVYAGSS LTSIVWNGVS LSATKTKYGS YSASLPGTES RVISLPSLTN WESANSLPEK
ETSYDDSKWT VCNKTTTLSP IAPLTLPVLF SSDYGFYTGQ KIYRGYFDGL TYTSINITCS
GGLAFGWSAW LNGVLIGGNT GVATATTTNA VLDLTNFTSV IKSENNLVTV VVDYHGHDET
STAKGVENPR GILGAFLVPK PSASTGFKLW KIQGNAGGSA NIDPVRGPMN EGGFYGERVG
WHLPSSPSLP SDSTPLIGLN TSGISFYTTN FTLALDSDLD VPLGIKLSAP AGTIARVMFW
INGYQYGKYV PHIGPQTVFP IPPGIINNQG SNKLALSLWA MTDAGARLTD VELVSYGVYE
SGFGFDRDWS YLQPGWDEGR LAYA
