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Database: UniProt
Entry: F9FJM9_FUSOF
LinkDB: F9FJM9_FUSOF
Original site: F9FJM9_FUSOF 
ID   F9FJM9_FUSOF            Unreviewed;       327 AA.
AC   F9FJM9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=4-hydroxy-2-oxoglutarate aldolase, mitochondrial {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOXB_06649 {ECO:0000313|EMBL:EGU82846.1};
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:EGU82846.1};
RN   [1] {ECO:0000313|EMBL:EGU82846.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU82846.1};
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 DapA family.
CC       {ECO:0000256|PIRNR:PIRNR001365}.
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:EGU82846.1}.
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DR   EMBL; AFQF01002021; EGU82846.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FJM9; -.
DR   STRING; 660025.F9FJM9; -.
DR   PaxDb; 5507-FOXG_05126P0; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd00408; DHDPS-like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR   PANTHER; PTHR12128:SF68; DIHYDRODIPICOLINATE SYNTHETASE; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|PIRNR:PIRNR001365}.
FT   ACT_SITE        152
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        181
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         58
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         226
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   327 AA;  34774 MW;  C099F53DF96EBF4D CRC64;
     MSAPPPKGIY VPVPTFFASK KTSNYNAITP PIDIETQVAH SVYLAKNGIK GLVVLGSTGE
     AVHIHPRDRH AILSGIKAGL EKEGFKDYPI IAGTATNSVE ETVEQLKDAQ KSGSQWGLCL
     VPGYNAGAVT QEGIIQWFTA VADQSPIPVM IYHYPGVSNN VKVAPSTYAT LAKHSNIVGC
     KLSHGDVSVA AQVASNPSID HTHFHCFTGL GQQLLPVISV GFAGAIDGSA GFFPKSLVRL
     FELSSKTQPT DAEIQERRLL QFKVSSMEEL VVKFGTVGIK DAISRLRGFG DTDGTRLPLV
     GGIPGGDAEW AKWKGVIGAV DEVEKSL
//
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