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Database: UniProt
Entry: K9FBM1_PEND1
LinkDB: K9FBM1_PEND1
Original site: K9FBM1_PEND1 
ID   K9FBM1_PEND1            Unreviewed;       326 AA.
AC   K9FBM1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Oxaloacetate hydrolase {ECO:0000313|EMBL:EKV05447.1};
GN   ORFNames=PDIP_83050 {ECO:0000313|EMBL:EKV05447.1};
OS   Penicillium digitatum (strain Pd1 / CECT 20795) (Green mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1170230 {ECO:0000313|EMBL:EKV05447.1, ECO:0000313|Proteomes:UP000009886};
RN   [1] {ECO:0000313|Proteomes:UP000009886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd1 / CECT 20795 {ECO:0000313|Proteomes:UP000009886};
RX   PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA   Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA   Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT   postharvest pathogen of citrus.";
RL   BMC Genomics 13:646-646(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate +
CC         succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30;
CC         Evidence={ECO:0000256|ARBA:ARBA00001050};
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:EKV05447.1}.
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DR   EMBL; AKCU01000501; EKV05447.1; -; Genomic_DNA.
DR   RefSeq; XP_014532462.1; XM_014676976.1.
DR   AlphaFoldDB; K9FBM1; -.
DR   SMR; K9FBM1; -.
DR   GeneID; 26236621; -.
DR   KEGG; pdp:PDIP_83050; -.
DR   HOGENOM; CLU_027389_3_0_1; -.
DR   OrthoDB; 554215at2759; -.
DR   Proteomes; UP000009886; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42905:SF2; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EKV05447.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
SQ   SEQUENCE   326 AA;  35470 MW;  DAFDCF9A38FF8E66 CRC64;
     MTITITVEKD GYYEVNGIRQ EPVVSLYVIP AASKLRRMLK DTKELIVCPG VYDGLSARIA
     MQVGFKGLYM TGAGTTASRL GMADLGLAQL HDMKTNAEMI ANLDPFGPPL IADMDTGYGG
     PLMVSKAVQQ YIQAGVAGFH IEDQIQNKRC GHLNGKKVVS LEEYLMRIRA AKLTKDRLHS
     DIVLIARTDA LQQHGYEECI RRLKAARDIG ADVGLLEGFT SKEQARQAVQ DLAPWPLLLN
     MVENGASPLI TTKEAEEMGF RIMIFSFATI TPAYMGIKAT LERLKADGVV GVPDGLGPRT
     IFEVCGLIDS MKVDTESGND GFAEGV
//
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