PRPC_FUSSL
ID PRPC_FUSSL Reviewed; 472 AA.
AC C7C435;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=2-methylcitrate synthase, mitochondrial {ECO:0000305};
DE Short=Methylcitrate synthase {ECO:0000303|PubMed:19661181};
DE EC=2.3.3.5 {ECO:0000269|PubMed:19661181};
DE AltName: Full=(2S,3S)-2-methylcitrate synthase {ECO:0000250|UniProtKB:P31660};
DE AltName: Full=Citrate synthase 2 {ECO:0000305};
DE EC=2.3.3.16 {ECO:0000269|PubMed:19661181};
DE Flags: Precursor;
GN Name=mcsA {ECO:0000303|PubMed:19661181};
OS Fusarium solani (Filamentous fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=169388;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=IP2330.95;
RX PubMed=19661181; DOI=10.1099/mic.0.031781-0;
RA Domin N., Wilson D., Brock M.;
RT "Methylcitrate cycle activation during adaptation of Fusarium solani and
RT Fusarium verticillioides to propionyl-CoA-generating carbon sources.";
RL Microbiology 155:3903-3912(2009).
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:19661181}.
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:19661181};
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:0000269|PubMed:19661181};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.94 uM for propionyl-CoA {ECO:0000269|PubMed:19661181};
CC KM=1.26 uM for acetyl-CoA {ECO:0000269|PubMed:19661181};
CC KM=2.58 uM for oxaloacetate (in presence of propionyl-CoA)
CC {ECO:0000269|PubMed:19661181};
CC KM=3.85 uM for propionyl-CoA (in presence of acetyl-CoA)
CC {ECO:0000269|PubMed:19661181};
CC pH dependence:
CC Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:19661181};
CC Temperature dependence:
CC Optimum temperature is 49-54 degrees Celsius.
CC {ECO:0000269|PubMed:19661181};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; FN400886; CAZ64274.1; -; mRNA.
DR AlphaFoldDB; C7C435; -.
DR SMR; C7C435; -.
DR PRIDE; C7C435; -.
DR UniPathway; UPA00946; -.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0050440; F:2-methylcitrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
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; 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 PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Mitochondrion; Transferase; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..472
FT /note="2-methylcitrate synthase, mitochondrial"
FT /evidence="ECO:0000312|EMBL:CAZ64274.1"
FT /id="PRO_5000565170"
FT ACT_SITE 307
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 353
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 410
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 347..351
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 436
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
SQ SEQUENCE 472 AA; 52072 MW; E29B1FFB208A5049 CRC64;
MALNLTTSRR ALGSLKPLTR AAFVGARGYA TAEPDLKATL REAIPAKREL LKKVKAHANK
TIGEVKVENT LGGMRGLKAM VWEGSVLDAN EGIRFHGRTI KDCQKELPKG KTGTEMLPEA
MFWLLLTGQV PSTNQIRVFS RELAEKAQIP EFVAKMLDNF PKDLHPMTQF AMAVSALNYE
SKFAKAYEQG LNKADYWEPT FDDCISLLAK LPTIAAKIYQ NSYRGGGALP AEVDLEQDWS
YNFAAMLGKG GKENENFQDL LRLYLALHGD HEGGNVSAHA THLVGSALSD PFLSYSAGLQ
GLAGPLHGLA AQEVLRWILQ MKEAIPAKYT EQDVNDYLWS TLNSGRVVPG YGHAVLRKPD
PRFEALMDYA AARPEIAQDP VFQLVQKNSQ IAPEVLKKHG KTKNPYPNVD SSSGVLFHHY
GFHETLYYTA TFGVSRGLGP LAQLVWDRAL GLPIERPKSI NLEGILKQVE GQ
