GenomeNet

Database: UniProt
Entry: F9F1J2_FUSOF
LinkDB: F9F1J2_FUSOF
Original site: F9F1J2_FUSOF 
ID   F9F1J2_FUSOF            Unreviewed;       571 AA.
AC   F9F1J2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Glycosyl hydrolase family 13 catalytic domain-containing protein {ECO:0000259|SMART:SM00642};
GN   ORFNames=FOXB_00167 {ECO:0000313|EMBL:EGU89214.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU89214.1};
RN   [1] {ECO:0000313|EMBL:EGU89214.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU89214.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(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}.
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:EGU89214.1}.
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DR   EMBL; AFQF01000085; EGU89214.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9F1J2; -.
DR   STRING; 660025.F9F1J2; -.
DR   PaxDb; 5507-FOXG_00152P0; -.
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   Maltose metabolism {ECO:0000256|ARBA:ARBA00026248}.
FT   DOMAIN          19..430
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   571 AA;  66132 MW;  39F3DBF3C5E0766A CRC64;
     MGSTDQSLRA WWKESSVYQV YPASYQDSTG SGVGDLKGII SRVDYLKDLG VDIVWLSPIF
     KSPQVDMGYD ISDYYTIDPP YGDVSDVDVL KDKLHERGMK LVLDLVMNHT SDQHEWFRES
     RKSKDNPYRD WYIWKPAKYD SEGNRHPPNN WDAHFQGSAW EYDETTDEYY LCLFCKQQPD
     LNWENPAVRK QVHDVMRFWL DRGTDGFRMD VINFVSKDQA FPDSDKTVLR GHEFYACGPR
     CHEFLKEIGA ILQEYDAFSV GEMPCVHDER ELIKAVRGDR GELSMIFHFE LMDLDHGVGG
     KFTPRSWDLS ELKSTTLKWQ KFMYDNEGWN ALYLENHDQP RAVSRFVHDD TEHRVDSAKL
     IAIFLGFQSG TPFIYQGQEI GMTNVPRDWD LEEYKDLDCL RHWDLHRNDD EAARNSYKVE
     YQKKSRDNAR TPMQWDASPN AGFTTADAKP WMRVNDNYKE INAASQTSDP NSVYGCYRKV
     LQRRKEFLDI FVYGNFQLVD ESNEKVFAYS RRAGNGETAL IVCNFTTDTV AWSLPGKTRE
     VLVSSAGRTV DDLNSGETKL APCEAFAVLL E
//
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