ID E3Q368_COLGM Unreviewed; 583 AA.
AC E3Q368;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Alpha amylase {ECO:0000313|EMBL:EFQ25047.1};
GN ORFNames=GLRG_00191 {ECO:0000313|EMBL:EFQ25047.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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; GG697331; EFQ25047.1; -; Genomic_DNA.
DR RefSeq; XP_008089067.1; XM_008090876.1.
DR AlphaFoldDB; E3Q368; -.
DR STRING; 645133.E3Q368; -.
DR EnsemblFungi; EFQ25047; EFQ25047; GLRG_00191.
DR GeneID; 24405556; -.
DR VEuPathDB; FungiDB:GLRG_00191; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_1_1_1; -.
DR OrthoDB; 3680211at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
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; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF222; MALTASE MALT (AFU_ORTHOLOGUE AFUA_8G07070); 1.
DR Pfam; PF00128; Alpha-amylase; 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 Maltose metabolism {ECO:0000256|ARBA:ARBA00026248};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782}.
FT DOMAIN 21..441
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 583 AA; 67504 MW; 86B1E2D5402E2F1A CRC64;
MGSITLNNPS RAWWKDGVIY QIYPASFKDA NGDGLGDVPG IISKVDYLKD LGVDIVWVSP
MYASPQIDMG YDISDYQDVH RPYGTVRDME VLIEECHKRG MKLILDLVVN HTSDQHKWFQ
ESRSSKENPK RNWYIWKPPR YAEDGTRLPP TNWRSHFSGS TWEWDETTGE YYLHLFAKEQ
PDLNWENEET REAIYDNAMR FWLDKGVDGF RIDTVNMYSK GVEFKDAPIM NKNAYEQPAY
MIYCNGPRIH EFLREMNAKV LNHYDTVTVG ELPHTPDPQH VLKYISAADR QLDMVFQFDI
VDLGQGIGYK YQTREWKLPE LKRIVAKWQQ FIEGTDGWTT AFCENHDQGR SVSRYGNDSP
QWRETSAKML ALMMCSQTGT LFVYQGQEIG MTNVSRSWGI EDYKDIEALN YYGDIKREHG
EGEVLSRVMD SINLVGRDNA RIPMQWDASP FAGFTDNKDG AWMRIHDEYA DINVAKQEAE
PSSVLNFWRE MLRLRKEEGE LLTHGAFELF DEENEQTFVY KKTRGGKSAV VALNFTSDEQ
EVRIPGEGSK IRVGNYGDVK ERVAAEGQKS VLRPWEGRLY LQG
//
