ID G4UQM6_NEUT9 Unreviewed; 315 AA.
AC G4UQM6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Phosphoenolpyruvate/pyruvate domain-containing protein {ECO:0000313|EMBL:EGZ71830.1};
GN ORFNames=NEUTE2DRAFT_110817 {ECO:0000313|EMBL:EGZ71830.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ71830.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ71830.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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; GL891236; EGZ71830.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UQM6; -.
DR STRING; 510952.G4UQM6; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_027389_3_0_1; -.
DR OMA; YDFLNYH; -.
DR Proteomes; UP000008513; 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 Pyruvate {ECO:0000313|EMBL:EGZ71830.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513}.
SQ SEQUENCE 315 AA; 33608 MW; 1A49705D25BDBB35 CRC64;
MAVINQAAAK LRAQLFESDD LIVCPGVQDG LSARVCLQQG FKNLYMTGAG TAISLLGMPD
LGLTTADDMV RQASMLSSLD RSVPLIADID TGFGGPVMVA RTVERYILGG VAGLHLEDQV
TTKRCGHLGG KEMVDVATFV ARIRAAREAR ERLGSDLVII ARTDALQSMG FDEALTRLKA
AVEAGADAVF LEGVKDREQM AKFTKAMAPT PCLINLVPGG LTPLVNAKEA KELGYRIAIW
PCFAMTHAYL AYQKAAKELL ETGAVTAGFT EKQKGEGESA EQVPGGIREL FELCGLSECV
EFDKKMGGQT FSKGV
//
