ID A0A484FLF4_COLOR Unreviewed; 927 AA.
AC A0A484FLF4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:TDZ18606.1};
GN Name=MAL2-2 {ECO:0000313|EMBL:TDZ18606.1};
GN ORFNames=Cob_v008588 {ECO:0000313|EMBL:TDZ18606.1};
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:TDZ18606.1, 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:TDZ18606.1}.
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DR EMBL; AMCV02000023; TDZ18606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A484FLF4; -.
DR STRING; 1213857.A0A484FLF4; -.
DR Proteomes; UP000014480; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000014480};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 837..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..442
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 798..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 104452 MW; 4719E52318485135 CRC64;
MGSVTVEKGD RAWWKDAVIY QIYPASFKDS NGDGLGDVPG IISKVDYLKD LGVDVVWVSP
MYASPQVDMG YDISDYQDVH RPYGTVQDME VLIDECHKRG MKLILDLVVN HTSDQHAWFK
ESRSSKTNPK RDWYIWKPPR YAEDGTRLPP TNWRSFFSGS TWEWDEATGE YYLHLFAVEQ
PDLNWENPET REAIYESAMR FWLDKGVDGF RVDTVNMYSK GVEWRDAPVV DESAYEQPAY
NIFCNGPRIH EFLREMNQKV LSHYDTVTVG ELPHTPDPQH VLRYVGAGDR QLDMVFQFDI
VDLGQGKICK YTAVDWTLPE LKRVVAKWQQ FVEGTDGWTT AFLENHDQGR SVSRYGSDAP
PWREPSAKML SLMNCAMTGT LFVYQGQEIG MVNVPRSWPI EDYKDIECRN FYSDFRREHG
EGSEFLEYVM DSINKLGRDN ARVPMQWDDS PYAGFTDCKT GAWMRVHELY PEINVARQER
EPKSVLNFWR AMLRLRKEEG ELLTHGAFEL FDEDNEKTFV FKKSRGGRAA VIALNFTSEE
QAVDVPGEGL VIRVGNYDDV KERVAQEGEK RVLRPWEGRL YLQDWSYVAN KLIWEFFLAC
TIVINIDTAT VIVAVLITIT ITITEPTTEP DLKRSLEFNP EFDLKHRSLG VGPLPRSICG
YYTLSGDPDI KTRSCEFGTT CGIASPNFSG LLACHTTVYT ECVVKKIFDP CPSVANPSET
AHPLCCQEKD GAIPVCRTYI GPRSNNPIAL KMYACEPTSL GHETNVFLYQ ETGYLLPQTR
SSGQTTGLTA NNLSSMTVSD ASTSGMTSTT GPLSTPTSTA TPAATSDVPS AQAQTPVIVG
GVIGGLVILG FVVCFVVWVR TRKPPAVSGP AELPGDQPVE HAGCELDAGG HRGRRREEEF
LMPESPVIRH FGNDDFHSVR QRSDLSP
//