ID F9FPK5_FUSOF Unreviewed; 312 AA.
AC F9FPK5; A0A0D2XXE9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=4-hydroxy-2-oxoglutarate aldolase, mitochondrial {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_08335 {ECO:0000313|EMBL:EGU81185.1};
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:EGU81185.1};
RN [1] {ECO:0000313|EMBL:EGU81185.1, ECO:0000313|Proteomes:UP000002489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU81185.1,
RC ECO:0000313|Proteomes:UP000002489};
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).
RN [2] {ECO:0000313|EnsemblFungi:FOXG_08665P0}
RP IDENTIFICATION.
RC STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936
RC {ECO:0000313|EnsemblFungi:FOXG_08665P0};
RG EnsemblFungi;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; AFQF01002499; EGU81185.1; -; Genomic_DNA.
DR STRING; 660025.F9FPK5; -.
DR PaxDb; 5507-FOXG_08665P0; -.
DR EnsemblFungi; FOXG_08665T0; FOXG_08665P0; FOXG_08665.
DR Proteomes; UP000002489; Unassembled WGS sequence.
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:SF52; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002489}.
FT ACT_SITE 150
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 179
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 221
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 312 AA; 32735 MW; DAD85B10C88975B7 CRC64;
MGSPKASQLR LGDGVYVPTL AFFTPEDEVD TSATEKHIIK LLESGVAGIV VHGSNGECAH
LSPSERTTII RVARDTIFHE GSGTRVPLIA GCGAQSTRET TELCEDAGKA GATHALVLPP
SYYGGLLPDD LVIQHYYTVA DKSPIPLLVY NFPGAAAGRD LSSDTILSIA KHPNVVGVKL
TCGNTGKLAR IAADCPEGFW VGGGSADFIL QGHAVGANGT ISGLANLCPK ACVRITELAE
EGNWKEARQL QAKVAKADWT AIKTGFVGVK AALGHFSGYG GEPRRPCVAP SQKDLDTIAQ
GFQEVMDLEV TL
//
