ID E4ZNJ5_LEPMJ Unreviewed; 463 AA.
AC E4ZNJ5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Citrate synthase {ECO:0000256|RuleBase:RU000441};
GN ORFNames=LEMA_P039550.1 {ECO:0000313|EMBL:CBX93054.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-methylcitrate +
CC CoA + H(+); Xref=Rhea:RHEA:23780, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:58853; EC=2.3.3.5;
CC Evidence={ECO:0000256|ARBA:ARBA00036244};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00000308};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005026}.
CC -!- SIMILARITY: Belongs to the citrate synthase family.
CC {ECO:0000256|ARBA:ARBA00010566, ECO:0000256|RuleBase:RU000441}.
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DR EMBL; FP929105; CBX93054.1; -; Genomic_DNA.
DR RefSeq; XP_003836419.1; XM_003836371.1.
DR AlphaFoldDB; E4ZNJ5; -.
DR STRING; 985895.E4ZNJ5; -.
DR EnsemblFungi; CBX93054; CBX93054; LEMA_P039550.1.
DR GeneID; 13282759; -.
DR eggNOG; KOG2617; Eukaryota.
DR HOGENOM; CLU_022049_2_1_1; -.
DR InParanoid; E4ZNJ5; -.
DR OMA; NEAAMDM; -.
DR OrthoDB; 3513214at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0050440; F:2-methylcitrate synthase activity; IEA:EnsemblFungi.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:EnsemblFungi.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:EnsemblFungi.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:EnsemblFungi.
DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR019810; Citrate_synthase_AS.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR PANTHER; PTHR11739:SF15; CITRATE SYNTHASE 3, MITOCHONDRIAL; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; Citrate synthase; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000441}.
SQ SEQUENCE 463 AA; 50671 MW; AF76746AE6B8493E CRC64;
MALSARTASR ALRSAKARPF ASVHACSYSS SSEPDLKETF KKVLPAKREL LKKVKAHADK
KLGDVKVENA LDFRGLKAMV WEGSVLDANE GIRFHGKTIK DCQKELPKGT SGTEMLPEAM
FWLLLTGEVP SVAQTRALSR ELAEKAAIPK FVEKMLDDFP KDLHPMTQFA CAVSALNYES
KFAKAYEKGI NKADYWEPTF DDSISLLAKL PTIAAKIYQN AYRGGGALPA EVDVEQDWAY
NFAAMLGKSG KENEGFQDLL RLYLALHGDH EGGNVSAHAT HLVGSALSDP FLSYSAGLQG
LAGPLHGLAA QEVLRFIIDM QKSVGEKFSE SDVKNYLWSV LKSGRVIPGY GHAVLRKPDP
RFEALMDFAN ARPDIAANPV YQLVKKNSEV APGTKNPFPN VDSSSGVLFH HYGFKETLYY
TATFGVSRGL GPLAQLIWDR ALGLPIERPK SINLQGILNQ VGA
//
