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2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) ((2S,3S)-2-methylcitrate synthase) (Citrate synthase) (EC 2.3.3.16)

 PRPC_SHEON              Reviewed;         375 AA.
Q8EJW2;
29-APR-2015, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 95.
RecName: Full=2-methylcitrate synthase {ECO:0000303|PubMed:14702315};
Short=2-MCS {ECO:0000303|PubMed:14702315};
Short=MCS {ECO:0000303|PubMed:14702315};
EC=2.3.3.5 {ECO:0000250|UniProtKB:P31660};
AltName: Full=(2S,3S)-2-methylcitrate synthase {ECO:0000250|UniProtKB:P31660};
AltName: Full=Citrate synthase {ECO:0000250|UniProtKB:P31660};
EC=2.3.3.16 {ECO:0000250|UniProtKB:P31660};
Name=prpC; OrderedLocusNames=SO_0344;
Shewanella oneidensis (strain MR-1).
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Shewanellaceae; Shewanella.
NCBI_TaxID=211586;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MR-1;
PubMed=12368813; DOI=10.1038/nbt749;
Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A.,
Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J.,
Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S.,
Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A.,
White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M.,
Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J.,
Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O.,
Venter J.C., Nealson K.H., Fraser C.M.;
"Genome sequence of the dissimilatory metal ion-reducing bacterium
Shewanella oneidensis.";
Nat. Biotechnol. 20:1118-1123(2002).
[2]
FUNCTION.
STRAIN=MR-1;
PubMed=14702315; DOI=10.1128/JB.186.2.454-462.2004;
Grimek T.L., Escalante-Semerena J.C.;
"The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a
new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires
prpF function in vivo.";
J. Bacteriol. 186:454-462(2004).
-!- FUNCTION: Involved in the catabolism of short chain fatty acids
(SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route)
and via the 2-methylcitrate cycle II (propionate degradation
route). Catalyzes the Claisen condensation of propionyl-CoA and
oxaloacetate (OAA) to yield (2S,3S)-2-methylcitrate (2-MC) and CoA
(PubMed:14702315). Catalyzes the condensation of oxaloacetate with
acetyl-CoA (By similarity). {ECO:0000250|UniProtKB:P31660,
ECO:0000269|PubMed:14702315}.
-!- CATALYTIC ACTIVITY: Propanoyl-CoA + H(2)O + oxaloacetate =
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA.
{ECO:0000250|UniProtKB:P31660}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate +
CoA. {ECO:0000250|UniProtKB:P31660}.
-!- PATHWAY: Organic acid metabolism; propanoate degradation.
{ECO:0000305}.
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
isocitrate from oxaloacetate: step 2/2. {ECO:0000305}.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P31660}.
-!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE014299; AAN53429.1; -; Genomic_DNA.
RefSeq; NP_715984.1; NC_004347.2.
RefSeq; WP_011070709.1; NC_004347.2.
ProteinModelPortal; Q8EJW2; -.
SMR; Q8EJW2; -.
STRING; 211586.SO_0344; -.
PaxDb; Q8EJW2; -.
EnsemblBacteria; AAN53429; AAN53429; SO_0344.
GeneID; 1168221; -.
KEGG; son:SO_0344; -.
PATRIC; fig|211586.12.peg.334; -.
eggNOG; ENOG4105BZN; Bacteria.
eggNOG; COG0372; LUCA.
HOGENOM; HOG000021225; -.
KO; K01659; -.
OMA; LTYCGYD; -.
OrthoDB; POG091H00T5; -.
PhylomeDB; Q8EJW2; -.
UniPathway; UPA00223; UER00718.
UniPathway; UPA00946; -.
Proteomes; UP000008186; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:UniProtKB.
GO; GO:0036440; F:citrate synthase activity; ISS:UniProtKB.
GO; GO:0016833; F:oxo-acid-lyase activity; ISS:TIGR.
GO; GO:0006113; P:fermentation; ISS:TIGR.
GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; TAS:UniProtKB.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.580.10; -; 2.
InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
InterPro; IPR002020; Citrate_synthase.
InterPro; IPR019810; Citrate_synthase_AS.
InterPro; IPR024176; Citrate_synthase_bac-typ.
InterPro; IPR036969; Citrate_synthase_sf.
PANTHER; PTHR11739; PTHR11739; 1.
Pfam; PF00285; Citrate_synt; 1.
PIRSF; PIRSF001369; Citrate_synth; 1.
PRINTS; PR00143; CITRTSNTHASE.
SUPFAM; SSF48256; SSF48256; 1.
TIGRFAMs; TIGR01800; cit_synth_II; 1.
PROSITE; PS00480; CITRATE_SYNTHASE; 1.
3: Inferred from homology;
Complete proteome; Reference proteome; Transferase;
Tricarboxylic acid cycle.
CHAIN 1 375 2-methylcitrate synthase.
/FTId=PRO_0000432971.
REGION 255 259 Coenzyme A binding.
{ECO:0000250|UniProtKB:O34002}.
ACT_SITE 222 222 {ECO:0000250|UniProtKB:O34002}.
ACT_SITE 261 261 {ECO:0000250|UniProtKB:O34002}.
ACT_SITE 312 312 {ECO:0000250|UniProtKB:O34002}.
BINDING 72 72 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 187 187 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 270 270 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 337 337 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 356 356 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
SEQUENCE 375 AA; 41431 MW; C41B9ED9842F7986 CRC64;
MSDAKKLTGA GLRGQSAGET ALSTVGVSGS GLTYRGYDVK DLAENATFEE VAYLILYGEL
PTTAQLAAYK TKLKGMRGLP QALKEVLERI PADAHPMDVM RTGCSMLGNL EAEHSFSEQS
QIADRLLAAF PSIICYWYRF SHDGVRIDTE TDDDQIGAHF LHLLHGKAPS ALHTKVMDVS
LILYAEHEFN ASTFTARVCA STLSDMHSCV TGAIGSLRGP LHGGANEAAM ELIQDMKDEA
DARDVLMGKL ERKEKIMGFG HAIYRDSDPR NAIIKEWSEK LAADYGDDRL YRVSVACEAL
MWEQKKLFCN ADFFHASAYH FMGIPTKLFT PIFVCSRVTG WTAHVMEQRS NNRIIRPSAD
YVGVSPRKVI PIANR


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