PRPC_YARLI
ID PRPC_YARLI Reviewed; 465 AA.
AC Q6C793;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=2-methylcitrate synthase, mitochondrial {ECO:0000305};
DE Short=Methylcitrate synthase {ECO:0000303|Ref.3};
DE EC=2.3.3.5 {ECO:0000269|PubMed:7117251, ECO:0000269|Ref.2, ECO:0000269|Ref.3};
DE AltName: Full=(2S,3S)-2-methylcitrate synthase {ECO:0000250|UniProtKB:Q9TEM3};
DE AltName: Full=Citrate synthase 2 {ECO:0000305};
DE EC=2.3.3.16 {ECO:0000269|Ref.3};
GN OrderedLocusNames=YALI0E02684g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX DOI=10.1271/bbb1961.39.2035;
RA Tabuchi T., Uchiyama H.;
RT "Methylcitrate condensing and methylisocitrate cleaving enzymes; evidence
RT for the pathway of oxidation of propionyl-CoA to pyruvate via C7-
RT tricarboxylic acids.";
RL Agric. Biol. Chem. 39:2035-2042(1975).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX DOI=10.1271/bbb1961.40.1411;
RA Uchiyama H., Tabuchi T.;
RT "Properties of methylcitrate synthase from Candida lipolytica.";
RL Agric. Biol. Chem. 40:1411-1418(1976).
RN [4]
RP SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7117251; DOI=10.1111/j.1432-1033.1982.tb06713.x;
RA Uchiyama H., Ando M., Toyonaka Y., Tabuchi T.;
RT "Subcellular localization of the methylcitric-acid-cycle enzymes in
RT propionate metabolism of Yarrowia lipolytica.";
RL Eur. J. Biochem. 125:523-527(1982).
CC -!- FUNCTION: Component of the methylcitrate cycle that catalyzes the
CC synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and
CC oxaloacetate. Plays an important role in detoxification of propionyl-
CC CoA, an inhibitor of both primary and secondary metabolism. Has also
CC citrate synthase activity using as substrates acetyl-CoA and
CC oxaloacetate. {ECO:0000269|PubMed:7117251, ECO:0000269|Ref.2,
CC ECO:0000269|Ref.3}.
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:0000269|PubMed:7117251, ECO:0000269|Ref.2,
CC ECO:0000269|Ref.3};
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; Evidence={ECO:0000269|Ref.3};
CC -!- ACTIVITY REGULATION: Activity is inhibited by p-chloromercuribenzoate
CC (pCMB), monoiodoacetamide, H(2)O(2), ATP, ADP, NADH, NADPH, Hg(2+) and
CC Zn(2+). {ECO:0000269|Ref.3}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.9 uM for acetyl-CoA {ECO:0000269|Ref.3};
CC KM=22 uM for butyryl-CoA {ECO:0000269|Ref.3};
CC KM=25 uM for oxaloacetate {ECO:0000269|Ref.3};
CC KM=5.3 uM for propionyl-CoA {ECO:0000269|Ref.3};
CC KM=25 uM for valeryl-CoA {ECO:0000269|Ref.3};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|Ref.3};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. {ECO:0000269|Ref.3};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:7117251}.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; CR382131; CAG79048.1; -; Genomic_DNA.
DR RefSeq; XP_503469.1; XM_503469.1.
DR AlphaFoldDB; Q6C793; -.
DR SMR; Q6C793; -.
DR STRING; 4952.CAG79048; -.
DR EnsemblFungi; CAG79048; CAG79048; YALI0_E02684g.
DR GeneID; 2912112; -.
DR KEGG; yli:YALI0E02684g; -.
DR VEuPathDB; FungiDB:YALI0_E02684g; -.
DR HOGENOM; CLU_022049_2_1_1; -.
DR InParanoid; Q6C793; -.
DR OMA; TVGWCAQ; -.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0050440; F:2-methylcitrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 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; IPR010109; Citrate_synthase_euk.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01793; cit_synth_euk; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Reference proteome; Transferase.
FT CHAIN 1..465
FT /note="2-methylcitrate synthase, mitochondrial"
FT /id="PRO_0000433357"
FT ACT_SITE 301
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 347
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 402
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 341..345
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 428
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
SQ SEQUENCE 465 AA; 51709 MW; B8393AE07D39D91A CRC64;
MISAIRPAVR SSVRVAPMAN TAFRAYSTQD GLKERFAELI PENVEKIKKL RKEKGNTVIG
EVILDQAYGG MRGIKGLVWE GSVLDPEEGI RFRGLTIPDL QKQLPHAPGG KEPLPEGLFW
LLLTGEIPTD AQVKGLSADW ASRAEIPKHV EELIDRCPPT LHPMAQLGIA VNALESESQF
TKAYEKGVNK KEYWQYTYED SMNLIAKLPV IASRIYRNLF KDGKIVGSID NSLDYSANFA
SLLGFGDNKE FIELLRLYLT IHADHEGGNV SAHTTKLVGS ALSSPFLSLS AGLNGLAGPL
HGRANQEVLE WILEMKSKIG SDVTKEDIEK YLWDTLKAGR VVPGYGHAVL RKTDPRYTAQ
REFALEHMPD YDLFHLVSTI YEVAPKVLTE HGKTKNPWPN VDSHSGVLLQ YYGLTEQSYY
TVLFGVSRAI GVLPQLIMDR AYGAPIERPK SFSTEKYAEL VGLKL
