ID S0EMB8_GIBF5 Unreviewed; 347 AA.
AC S0EMB8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Related to dihydrodipicolinate synthase {ECO:0000313|EMBL:CCT75762.1};
GN ORFNames=FFUJ_11799 {ECO:0000313|EMBL:CCT75762.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT75762.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; HF679033; CCT75762.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EMB8; -.
DR STRING; 1279085.S0EMB8; -.
DR EnsemblFungi; CCT75762; CCT75762; FFUJ_11799.
DR VEuPathDB; FungiDB:FFUJ_11799; -.
DR HOGENOM; CLU_049343_0_2_1; -.
DR OrthoDB; 1780992at2759; -.
DR Proteomes; UP000016800; Chromosome 11.
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:SF47; DIHYDRODIPICOLINATE SYNTHETASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_2G01230); 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:UP000016800}.
FT ACT_SITE 154
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 192
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 235
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 347 AA; 37227 MW; 8388C9D1DCFE22D2 CRC64;
MAKEVSSSQI FVPTRTLPFN PGVWCPAVTF FNHSDDTVDH ASQAKYFAHL ADSGLNGLIV
MGSNAEAFLL TREERYELIA LARKTIGPDF PLMAGVGAHS TKQTLELAED AHKAGANYLL
VLPPAYFGKA TSMNVVKRFF SEVAKKSPLP VVIYNFPGVT NGVDIDSETI VQIYEESKKS
HPSGKSNVVG VKLTCGSVGK ITRLAAQIPS SEFSTYGGQS DFLIGGLAAG SVGCVAAFAN
VFPTLTSKIY ALYKEGKFDE ALKLQQLAAL AERPCKAGVA STKYAVAVFS ARLAGVEGAE
EKLAPRHPYE PVGEAVKTSV QSIMKEAGDK EEELLKTWTD RVKGRLN
//
