BGALB_BOTFB
ID BGALB_BOTFB Reviewed; 1007 AA.
AC A6RPN7;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=BC1G_02410;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
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}.
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DR EMBL; CH476848; EDN31260.1; -; Genomic_DNA.
DR RefSeq; XP_001559246.1; XM_001559196.1.
DR AlphaFoldDB; A6RPN7; -.
DR SMR; A6RPN7; -.
DR VEuPathDB; FungiDB:Bcin06g04500; -.
DR OMA; GHQSKII; -.
DR OrthoDB; 179316at2759; -.
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; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1007
FT /note="Probable beta-galactosidase B"
FT /id="PRO_0000395228"
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 155
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 409
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 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 815
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 268..321
FT /evidence="ECO:0000250"
SQ SEQUENCE 1007 AA; 110544 MW; B78768183EDEE67F CRC64;
MRLQSLFASA LTLGSCVAQN STNGTWPIHN NGLTTQIEWD HYSMIVNGQR FFLWSGELHY
WRIPVPELWV DVLQKIKAAG FNTFAIYTHW YFHNPNPETL DFENAAHDFT KIFDLAKELG
MYVVFRPGPY VNAESNAGAF PLWLTTGAYG SLRNNDTRYT EAWTPFWEKV ASIVAPYQLT
NGGNVLTYQI ENELGSQWRG TPSKKIPNLS SIQYMEALEA SARAQGITIP FQANDPNLNS
DSWSKDFYDG YGSVDIYGMD SYPACWTCNL TECDSTNGAY KPFNVIDYYD HFQEISPTQP
SFLPEFQGGS FNPWGGPEGG CPENSPADFA NLFYRNNVGQ RVTAMSLYML YGGTNWGWLA
APVVATSYDY SSPISENRMI NDKYAETKLF GQFLRVAKDL TKTDRIGTNQ TASTNPNIVY
SEIRNPDTNG AFYVTIHQES TVGTREEFYI NANTSKGEFT IPQKAAPIVL NGFQSKIIVT
DFSFGSHSLL YSTAEVLSHS IVDEEDILAL WMPTGEAGEF VVTGAKSGKV SSCGGCSSVG
FYPQGDDLLV TISQSEGISI LTFDDGLRVL VMDRSYAYEF WVPVLTADPF SPANETVFVQ
GPSLVRSVAY SSDGTILELT GDNNGTSTQI EVFPPKAVSE VTWNGQSIKT SKTDYGSLIG
SLTAPALDSL TLPEISGWKA NDSLPERLST YDDSWWVDAN HMNTSNPTKP ETLPVLYIDD
YGYHVGNHLW RGRFEGSASG VYLSVTGGRA FGYSAWLNGE FIGSYVGAAY PDTGELTLSF
GNLASSNSTN ILLVLQDNSG HDETSGALNP RGINNATLIS SSAKNFTSWK VTGTAGKPDT
AIDPVRGILS EGGLYAERLG WHLPGFDDSE WSSASPSNIS SSAGVTFYRT TVPLAIPTGL
DVAISFTLNA SPSNAALRAL LFVNGYQYGR FSPWIGNQIE FPVPPGILNY DGDNVIGLSV
WRQEEGGESM GVDVGWKITE AFASSFEPIF DATYLQPGWT EERLQYA
