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

 PRPC_MYCTE              Reviewed;         393 AA.
H8F0D7;
29-APR-2015, integrated into UniProtKB/Swiss-Prot.
16-MAY-2012, sequence version 1.
28-FEB-2018, entry version 38.
RecName: Full=2-methylcitrate synthase {ECO:0000303|PubMed:16689789};
Short=2-MCS {ECO:0000303|PubMed:16689789};
Short=MCS {ECO:0000303|PubMed:16689789};
EC=2.3.3.5 {ECO:0000269|PubMed:16689789};
AltName: Full=(2S,3S)-2-methylcitrate synthase {ECO:0000250|UniProtKB:P31660};
AltName: Full=Citrate synthase {ECO:0000303|PubMed:16689789};
Short=CS {ECO:0000303|PubMed:16689789};
EC=2.3.3.16 {ECO:0000269|PubMed:16689789};
Name=gltA1; OrderedLocusNames=ERDMAN_1267; ORFNames=Q643_01184;
Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=652616;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=22535945; DOI=10.1128/JB.00353-12;
Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
"Complete annotated genome sequence of Mycobacterium tuberculosis
Erdman.";
J. Bacteriol. 194:2770-2770(2012).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35801 / TMC 107 / Erdman;
The Broad Institute Genomics Platform;
The Broad Institute Genome Sequencing Center for Infectious Disease;
Earl A.M., Hung D., Gomez D., Hsueh P.R., Rozo J.C., Zambrano M.M.,
Desjardins C., Abeel T., Young S., Zeng Q., Gargeya S., Abouelleil A.,
Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Murphy C.,
Naylor J., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
"The genome sequence of Mycobacterium tuberculosis Erdman.";
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, INDUCTION, AND
SUBSTRATE SPECIFICITY.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=16689789; DOI=10.1111/j.1365-2958.2006.05155.x;
Munoz-Elias E.J., Upton A.M., Cherian J., McKinney J.D.;
"Role of the methylcitrate cycle in Mycobacterium tuberculosis
metabolism, intracellular growth, and virulence.";
Mol. Microbiol. 60:1109-1122(2006).
-!- 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 I (propionate degradation
route). Catalyzes the Claisen condensation of propionyl-CoA and
oxaloacetate (OAA) to yield (2S,3S)-2-methylcitrate (2-MC) and
CoA. Also catalyzes the condensation of oxaloacetate with acetyl-
CoA. {ECO:0000269|PubMed:16689789}.
-!- CATALYTIC ACTIVITY: Propanoyl-CoA + H(2)O + oxaloacetate =
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA.
{ECO:0000269|PubMed:16689789}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate +
CoA. {ECO:0000269|PubMed:16689789}.
-!- PATHWAY: Organic acid metabolism; propanoate degradation.
{ECO:0000305|PubMed:16689789}.
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
isocitrate from oxaloacetate: step 2/2.
{ECO:0000305|PubMed:16689789}.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:I6Y9Q3}.
-!- INDUCTION: By propionate, but not by glucose.
{ECO:0000269|PubMed:16689789}.
-!- DISRUPTION PHENOTYPE: Cells lacking both prpC and prpD are unable
to grow on propionate media in vitro or in murine bone marrow-
derived macrophages infected ex vivo. Paradoxically, bacterial
growth and persistence, and tissue pathology, are
indistinguishable in mice infected with wild-type.
{ECO:0000269|PubMed:16689789}.
-!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AP012340; BAL65070.1; -; Genomic_DNA.
EMBL; JLBG01000002; KBK19227.1; -; Genomic_DNA.
RefSeq; WP_003405909.1; NZ_KK339487.1.
ProteinModelPortal; H8F0D7; -.
SMR; H8F0D7; -.
EnsemblBacteria; BAL65070; BAL65070; ERDMAN_1267.
EnsemblBacteria; KBK19227; KBK19227; Q643_01184.
KEGG; mtn:ERDMAN_1267; -.
PATRIC; fig|652616.3.peg.1285; -.
KO; K01647; -.
OrthoDB; POG091H00T5; -.
UniPathway; UPA00223; UER00718.
UniPathway; UPA00946; -.
Proteomes; UP000007568; 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; IDA:UniProtKB.
GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IDA:UniProtKB.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.230.10; -; 1.
Gene3D; 1.10.580.10; -; 2.
InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
InterPro; IPR016143; Citrate_synth-like_sm_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.
1: Evidence at protein level;
Complete proteome; Transferase; Tricarboxylic acid cycle.
CHAIN 1 393 2-methylcitrate synthase.
/FTId=PRO_0000432970.
REGION 275 279 Coenzyme A binding.
{ECO:0000250|UniProtKB:O34002}.
ACT_SITE 242 242 {ECO:0000250|UniProtKB:O34002}.
ACT_SITE 281 281 {ECO:0000250|UniProtKB:O34002}.
ACT_SITE 332 332 {ECO:0000250|UniProtKB:O34002}.
BINDING 92 92 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 207 207 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 290 290 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 357 357 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 376 376 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
SEQUENCE 393 AA; 42969 MW; 5591E9F482CF1232 CRC64;
MTGPLAAARS VAATKSMTAP TVDERPDIKK GLAGVVVDTT AISKVVPQTN SLTYRGYPVQ
DLAARCSFEQ VAFLLWRGEL PTDAELALFS QRERASRRVD RSMLSLLAKL PDNCHPMDVV
RTAISYLGAE DPDEDDAAAN RAKAMRMMAV LPTIVAIDMR RRRGLPPIAP HSGLGYAQNF
LHMCFGEVPE TAVVSAFEQS MILYAEHGFN ASTFAARVVT STQSDIYSAV TGAIGALKGR
LHGGANEAVM HDMIEIGDPA NAREWLRAKL ARKEKIMGFG HRVYRHGDSR VPTMKRALER
VGTVRDGQRW LDIYQVLAAE MASATGILPN LDFPTGPAYY LMGFDIASFT PIFVMSRITG
WTAHIMEQAT ANALIRPLSA YCGHEQRVLP GTF


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