ID M7TT70_BOTF1 Unreviewed; 323 AA.
AC M7TT70;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative glycoside hydrolase family 43 protein {ECO:0000313|EMBL:EMR86781.1};
GN ORFNames=BcDW1_4589 {ECO:0000313|EMBL:EMR86781.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR86781.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; KB707847; EMR86781.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TT70; -.
DR STRING; 1290391.M7TT70; -.
DR HOGENOM; CLU_009397_4_1_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18619; GH43_CoXyl43_like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187}.
FT SITE 135
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 323 AA; 36657 MW; 9D64712C3F996AC3 CRC64;
MSEKEPLITH IYTADPSANV FNNTLYIYPS HDIPTDIQDN DNGDQYAMED YHVFSMSSIP
GEVTDHGVVL SNSSVPWASK QLWAPDACSK NGKYYLYFPA RDHDGIFRIG VAESDKPEGP
FTPDESYIPG SYSIDPCSFV DDDGEAYVYF GGIWGGQLQC WGNQHEVFER EKYSTMEPTT
GSALGPRVGK LSEDMHSFSS PVQEISILDE KTGEKLGADD HDRRFFEASW VHKYKGKYYF
SYSTGDTHYL CYAVGDKPEG PFVYKGRLLE PVVGWTTHHS IVEFQGRWWL FYHDSTLSGG
KNHLRCVKVR EIFYDEDGGM KVE
//
