ID F9FZJ6_FUSOF Unreviewed; 338 AA.
AC F9FZJ6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Endo-arabinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_11828 {ECO:0000313|EMBL:EGU77653.1};
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:EGU77653.1};
RN [1] {ECO:0000313|EMBL:EGU77653.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU77653.1};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:EGU77653.1}.
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DR EMBL; AFQF01002932; EGU77653.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FZJ6; -.
DR STRING; 660025.F9FZJ6; -.
DR PaxDb; 5507-FOXG_01604P0; -.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd08999; GH43_ABN-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..338
FT /note="Endo-arabinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003383389"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 181
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 338 AA; 37133 MW; 2FF845A8114842EC CRC64;
MPVSSSLWGR IIFFILSVFL FDTASALPAN ISSPVLRPFV LPPPKQHLSR RHKGRDKSFS
PRLDVNFPDP CLVQDQDDHW VSFATSGGGY HIQVAVADDL FGEWTHLQQD ALPGDGWTSG
RNYWAPDVRK LEDDSYIMYF SGELPEGGHC IGVARSHNST GPYTMDPKPF ACPRDEGGAI
DPAGFFDEST NKRYVVYKVD GNALNNGSGT PIRLQEVSTK DGSTPIGKPV DILDRIASED
GPLVEAPSLV RTEQGKYLLF FSSHMYTGDA YDVKWAMSDR VEGPYTRGSS PFLKTPALGL
KGPGGGTSSE NGQFMVFHAW CGKGKRCMYA IGYGLDYE
//
