ID S0EA89_GIBF5 Unreviewed; 311 AA.
AC S0EA89;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Related to 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase {ECO:0000313|EMBL:CCT70667.1};
GN ORFNames=FFUJ_06657 {ECO:0000313|EMBL:CCT70667.1};
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:CCT70667.1, 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 HpcH/HpaI aldolase family.
CC {ECO:0000256|ARBA:ARBA00005568}.
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DR EMBL; HF679028; CCT70667.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EA89; -.
DR EnsemblFungi; CCT70667; CCT70667; FFUJ_06657.
DR VEuPathDB; FungiDB:FFUJ_06657; -.
DR HOGENOM; CLU_059964_4_0_1; -.
DR OrthoDB; 1822991at2759; -.
DR Proteomes; UP000016800; Chromosome 6.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800}.
FT DOMAIN 32..247
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT REGION 272..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 32810 MW; 463FE85519E7ED3F CRC64;
MAAPIPHPMR EKLLRDEVAY TMSIKLVKSI EIAGMAKTAG YDGILVDMEH SSFDLETTNQ
LCVAALYAGI SPIVRAPSKD PFFVSRILDG GALGIIVPHI RSVQDAQDVV NAAKFQPIGH
RSSTNGLPHH QFRSIPAKVS NPVTNAATMV IPMIETLEAL ELVDEIAALP GVDSLLIGTN
DLTAEMGIPG DYENPRVTEA YERTIAACKK HGKWLGVGGL HARLDLVEKF CKMGARWVMA
ATDGPLLLGA ATKRGTEMAA LNASVVKSQQ ANGHSVEKKA TNGVTNGTTN GAVTNSNGIT
NGATNGIPVA A
//
