ID G2YVR5_BOTF4 Unreviewed; 585 AA.
AC G2YVR5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Glycoside hydrolase family 13 protein {ECO:0000313|EMBL:CCD55713.1};
GN ORFNames=BofuT4P176000001001 {ECO:0000313|EMBL:CCD55713.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD55713.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., 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., Guldener 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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; FQ790357; CCD55713.1; -; Genomic_DNA.
DR AlphaFoldDB; G2YVR5; -.
DR STRING; 999810.G2YVR5; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_2_3_1; -.
DR InParanoid; G2YVR5; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF232; GLYCOSYL HYDROLASE FAMILY 13 CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CCD55713.1};
KW Maltose metabolism {ECO:0000256|ARBA:ARBA00026248};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177}.
FT DOMAIN 23..446
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 585 AA; 67460 MW; 06330F25B6AC9C14 CRC64;
MGSIARRTIG STPQWWKEAV VYQIYPASYL DTTGSGDGDL NGITSKLPYI RSLGVDVVWI
SPIYASPMND MGYDISDYRA INPMFGTMED WERLCARAHE LGLKLVMDLV VNHTSSEHPW
FKESVSGGPN GPKRDFYYWQ PPKNGKEPNN WGAMFGGSSW EKDPSHQTDE YYLHVYDVSQ
PDLNWTNPAV RNEVWDIMRF WLDKGCDGFR MDVINCISKE PGFPDFEVTD PRLEFQIGVR
GNFNGPHVKE YLEEMHREVL CHYPEAFTVG ETPGLKRPES ALGLVQGGKP LQMIFQFEHM
YFDIQPGMKP FFPRPSWNLT EIKKNLGEWM SFNAAHDGWD SLYLENHDQP RILGRWAKDT
PEWRVQAAKM LALFHATGRG TLFVYQGQEI GTANSKWWTN EEFRDVEEIN FFAAEKERRE
KESNGKEVDM TDISRGIQGY GRDNSRMGMQ WNDSPNGGFT QGKPWIKTNE EYKEINVAAQ
DGVKGSTLEF WKQIIKLRKE NPVLCKGGFE MVDQENEEVY AYVRKGEEKE YLIACNFKER
DVKWKIPVET GELLFGSYED GVQGGEKEGE LNLRPFEGRI YVRDI
//
