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Database: UniProt
Entry: N4VK77_COLOR
LinkDB: N4VK77_COLOR
Original site: N4VK77_COLOR 
ID   N4VK77_COLOR            Unreviewed;       580 AA.
AC   N4VK77;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:TDZ20965.1};
GN   Name=MAL2-1 {ECO:0000313|EMBL:TDZ20965.1};
GN   ORFNames=Cob_v006222 {ECO:0000313|EMBL:TDZ20965.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS   414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum orbiculare species complex.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ20965.1, ECO:0000313|Proteomes:UP000014480};
RN   [1] {ECO:0000313|Proteomes:UP000014480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=23252678; DOI=10.1111/nph.12085;
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT   stage shift of Colletotrichum fungi.";
RL   New Phytol. 197:1236-1249(2013).
RN   [2] {ECO:0000313|Proteomes:UP000014480}
RP   GENOME REANNOTATION.
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA   Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA   Shirasu K.;
RT   "Genome sequence resources for four phytopathogenic fungi from the
RT   Colletotrichum orbiculare species complex.";
RL   Mol. Plant Microbe Interact. 32:1088-1090(2019).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TDZ20965.1}.
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DR   EMBL; AMCV02000016; TDZ20965.1; -; Genomic_DNA.
DR   AlphaFoldDB; N4VK77; -.
DR   STRING; 1213857.N4VK77; -.
DR   EnsemblFungi; ENH84202; ENH84202; Cob_07432.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_2_3_1; -.
DR   OrthoDB; 3680211at2759; -.
DR   Proteomes; UP000014480; 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:SF232; GLYCOSYL HYDROLASE FAMILY 13 CATALYTIC DOMAIN-CONTAINING PROTEIN; 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:UP000014480}.
FT   DOMAIN          20..439
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   580 AA;  67113 MW;  377056DD7567E5E4 CRC64;
     MTVITGPPER KWWKEAVVYQ IYPASFLDTD GDGLGDLPGI ISKLDYIKSV GANTIWLSPI
     FKSPQKDMGY DISDYRDIHR PYGTVQDVEA LIQGCHDRDI KLLLDLVVNH TSDQHEWFRE
     SRSSPSSPKR DWYFWRDPKY DADGNRRPPN NWASIFGGSA WHWDEHTGQY YLALFLPSQP
     DLNWSTDAMR QAAYADMEFW LGKGVDGFRI DSMNLMSKHP DLPDAPITLP GAEFQPGSLY
     YASGPRMHEY IREMRERVFD KYDCMTVGEL GFTKDEASVA SYVARDRHEL NMLFTGDIVD
     MDFEINKKYE HKDFRLSALK KITKLWQGAM VRCDGWNTIY MDNHDSGRSL TRYASDLPQF
     RRRAAKMLAT YLSTLSGTLF LLQGQEIGMA NIPESWPIEE YIDVEGRNYY ESERRRRGSD
     ADMSDLLKEM RLKARDNGRL PMQWSPKRHG GFTEGQKPWM RVNDDYPEWN VEKQDKDDSS
     VLAFWRDILD LRRKEKDVFV YGKFSEVAGF ENSEEVFVYT MKSYKGRCAL VALNFSDSQQ
     LVELESGFTG WKRLLTTNGE SIESGGVRLE AFEGALFASW
//
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