BGALB_SCLS1
ID BGALB_SCLS1 Reviewed; 1008 AA.
AC A7EBU5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Probable beta-galactosidase B;
DE EC=3.2.1.23;
DE AltName: Full=Lactase B;
DE Flags: Precursor;
GN Name=lacB; ORFNames=SS1G_02781;
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; CH476623; EDN99923.1; -; Genomic_DNA.
DR RefSeq; XP_001596561.1; XM_001596511.1.
DR AlphaFoldDB; A7EBU5; -.
DR SMR; A7EBU5; -.
DR STRING; 665079.A7EBU5; -.
DR EnsemblFungi; EDN99923; EDN99923; SS1G_02781.
DR GeneID; 5492844; -.
DR KEGG; ssl:SS1G_02781; -.
DR VEuPathDB; FungiDB:sscle_04g037140; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_1_1; -.
DR InParanoid; A7EBU5; -.
DR OMA; GHQSKII; -.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1008
FT /note="Probable beta-galactosidase B"
FT /id="PRO_0000395233"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 305
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 268..321
FT /evidence="ECO:0000250"
SQ SEQUENCE 1008 AA; 110685 MW; 52E5C90A03793D5E CRC64;
MLLQSLFAWA LAIGPCIAQN STNSTWPIHN NGLTTQVEWD HYSLMVDGQR FFLWSGEFHY
WRIPVPELWV DVLQKVKAAG FNTFAIYTHW YFHNPNPNTL DFENAAHNFT KIFDLAKELG
MFVVFRPGPY VNAESNAGAF PLWLTTGAYG ALRNNDERYT EAWTPFWEKV ASIVAPYQFT
NGGNVLTYQI ENELGSQWRG TPSNKVPNLS SVEYMEALEA SARAHGITIP FQANDPNLNS
DSWSKDFYDG YGSVDIYGMD SYPACWTCNL TECDSTNGAY KAFNVIDYYD HFEAISPTQP
SFLPEFQGGS FNPWGGPEGG CPENSPADFA NLFYRNNVGQ RVTAMSLYMI YGGTNWGWLA
APVVATSYDY SSPISENRMI NDKYAETKLF GHFLRVAKDL TKTDRIGTGK TASTNPNVVY
SEIRNPDTNA AFYVTIHKES TVGTREEFYI NANTSKGAFK IPQKAASIVL NGFQSKIIVT
DFNFGSHSLL YSTAEVLSHS IVDDQDILAL WMPTGEAGEF VVTGAKSGSV SSCGGCSSVG
FYPQGDDLLV TISQSKGISV LTFDDGLRVL VMDRSFAYEF WVPVLTADPF SPANETVFVQ
GPSLVRSAAY SSDGSTLDLT GDNNGTSTQI QVFPPKSVSK VTWNGQVITT EKTDYDSLIG
SLTGPALDSL TLPTISGWKA NDSLPERLPT YDDSWWVAAD HMNTSNPTKP ETLPVLYIDD
YGYHVGNHLW RGRFEGSASG VYLSVTGGRA FGYSAWLNGE FIGSYLGAAY PDTGKLTLSF
SNVTVNSNST NILLVLQDNS GHDETSEALN PRGINNATLI SSSTKNFTSW KVTGTAGKPD
TAIDPVRGIL SEGGLYAERL GWHLPDFDDS EWSSASPSNV SSSAGVTFYR TTVSLAIPTG
LDVAISFTLK ASPSNAALRV LLFVNGYQYG RFSPWIGNQV EFPVPPGILN YDGDNVIGLS
VWRQEEGDES MGVNVGWKVT EAFASSFEPI FDAAYLQPGW TDERLQYA
