ID   A0A1V6TQ24_9EURO        Unreviewed;       305 AA.
AC   A0A1V6TQ24;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQE28457.1};
GN   ORFNames=PENSTE_c003G09055 {ECO:0000313|EMBL:OQE28457.1};
OS   Penicillium steckii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE28457.1, ECO:0000313|Proteomes:UP000191285};
RN   [1] {ECO:0000313|Proteomes:UP000191285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE28457.1}.
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DR   EMBL; MLKD01000003; OQE28457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6TQ24; -.
DR   STRING; 303698.A0A1V6TQ24; -.
DR   OrthoDB; 554215at2759; -.
DR   Proteomes; UP000191285; Unassembled WGS sequence.
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:SF15; PHOSPHONOMUTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G03820)-RELATED; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191285}.
SQ   SEQUENCE   305 AA;  32412 MW;  A8FCA69CC9D3FCF3 CRC64;
     MALPSAATNL RRTLADPNGF VVAPGVYDGM SARLALAAGF DALYMTGAGT AASVHGQADL
     GICTLNDMRA NAEMLANLSP STPLIADADT GYGGPIMVAR TTEQYARSGV AGFHIEDQVQ
     TKRCGHLSGK LLVDKEAYTT RIRAAVQARQ RLGSDIVVIA RTDALQSHGY EESLARLRSA
     RDAGADVGFL EGITSREMAR QAVQDLAPWP LLLNMVEHGS TPNISAAEAR ELGFRIIIFP
     FATIGPALTA MREGLEKLKR DGIPGLDKEL TPQMLFRVCG LDRSVQLDAE AGGSAFDGGV
     DLREK
//