ID S8B8M0_PENO1 Unreviewed; 326 AA.
AC S8B8M0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPS31107.1};
GN ORFNames=PDE_06062 {ECO:0000313|EMBL:EPS31107.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS31107.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS31107.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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};
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DR EMBL; KB644413; EPS31107.1; -; Genomic_DNA.
DR AlphaFoldDB; S8B8M0; -.
DR STRING; 933388.S8B8M0; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_027389_3_0_1; -.
DR OrthoDB; 554215at2759; -.
DR PhylomeDB; S8B8M0; -.
DR Proteomes; UP000019376; 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: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 Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376}.
SQ SEQUENCE 326 AA; 35461 MW; 52043C05D57DACB7 CRC64;
MAITITVEKD GFYEVNGTRQ EPNVSLYVIP AASKLRRMLK DSKELIVCPG VYDGLSARIA
MELGFKAMYM TGAGTTASRL GMADLGLAQL HDMRTNAEMI ANLDPFGPPL IADMDTGYGG
PLMVSKSVQQ YIQAGVAGFH IEDQIQNKRC GHLAGKKVVS REEYMTRIRA AKLTKERLHS
DIVLIARTDA LQQHGYEECI ERLKAARDLG ADVGLLEGFT SKEQARQAVQ DLAPWPLLLN
MVENGATPII TTKEAQEMGF RIMIFSFASL APAYLGIRAS FQRLLTEGVV GTPEGLSPRK
LFEVCGLSES IKVDTEAGGD GFANGV
//
