ID   PRPD_MYCTE              Reviewed;         505 AA.
AC   H8F0D6;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=2-methylcitrate dehydratase {ECO:0000303|PubMed:16689789};
DE            Short=2-MC dehydratase {ECO:0000303|PubMed:16689789};
DE            EC=4.2.1.79 {ECO:0000269|PubMed:16689789};
DE   AltName: Full=Aconitate hydratase {ECO:0000250|UniProtKB:P77243};
DE            Short=ACN {ECO:0000250|UniProtKB:P77243};
DE            Short=Aconitase {ECO:0000250|UniProtKB:P77243};
DE            EC=4.2.1.3 {ECO:0000250|UniProtKB:P77243};
GN   OrderedLocusNames=ERDMAN_1266;
OS   Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=652616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=22535945; DOI=10.1128/jb.00353-12;
RA   Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT   "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL   J. Bacteriol. 194:2770-2770(2012).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND INDUCTION.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=16689789; DOI=10.1111/j.1365-2958.2006.05155.x;
RA   Munoz-Elias E.J., Upton A.M., Cherian J., McKinney J.D.;
RT   "Role of the methylcitrate cycle in Mycobacterium tuberculosis metabolism,
RT   intracellular growth, and virulence.";
RL   Mol. Microbiol. 60:1109-1122(2006).
CC   -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC       via the tricarboxylic acid (TCA)(acetyl degradation route) and via the
CC       2-methylcitrate cycle I (propionate degradation route). Catalyzes the
CC       dehydration of 2-methylcitrate (2-MC) to yield the cis isomer of 2-
CC       methyl-aconitate (PubMed:16689789). Could also catalyze the dehydration
CC       of citrate and the hydration of cis-aconitate (By similarity).
CC       {ECO:0000250|UniProtKB:P77243, ECO:0000269|PubMed:16689789}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3S)-2-methylcitrate = 2-methyl-cis-aconitate + H2O;
CC         Xref=Rhea:RHEA:17725, ChEBI:CHEBI:15377, ChEBI:CHEBI:57872,
CC         ChEBI:CHEBI:58853; EC=4.2.1.79;
CC         Evidence={ECO:0000269|PubMed:16689789};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC         ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC         Evidence={ECO:0000250|UniProtKB:P77243};
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000305|PubMed:16689789}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 1/2. {ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P77243}.
CC   -!- INDUCTION: By propionate, but not by glucose.
CC       {ECO:0000269|PubMed:16689789}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking both prpC and prpD are unable to
CC       grow on propionate media in vitro or in murine bone marrow-derived
CC       macrophages infected ex vivo. Paradoxically, bacterial growth and
CC       persistence, and tissue pathology, are indistinguishable in mice
CC       infected with wild-type. {ECO:0000269|PubMed:16689789}.
CC   -!- SIMILARITY: Belongs to the PrpD family. {ECO:0000305}.
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DR   EMBL; AP012340; BAL65069.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8F0D6; -.
DR   SMR; H8F0D6; -.
DR   EnsemblBacteria; BAL65069; BAL65069; ERDMAN_1266.
DR   KEGG; mtn:ERDMAN_1266; -.
DR   PATRIC; fig|652616.3.peg.1284; -.
DR   HOGENOM; CLU_026574_3_0_11; -.
DR   UniPathway; UPA00223; UER00717.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000007568; Chromosome.
DR   GO; GO:0047547; F:2-methylcitrate dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IDA:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.4100.10; -; 1.
DR   Gene3D; 3.30.1330.120; -; 1.
DR   InterPro; IPR036148; MmgE/PrpD_sf.
DR   InterPro; IPR042183; MmgE/PrpD_sf_1.
DR   InterPro; IPR042188; MmgE/PrpD_sf_2.
DR   InterPro; IPR005656; MmgE_PrpD.
DR   InterPro; IPR045337; MmgE_PrpD_C.
DR   InterPro; IPR045336; MmgE_PrpD_N.
DR   PANTHER; PTHR16943; PTHR16943; 1.
DR   Pfam; PF03972; MmgE_PrpD; 1.
DR   Pfam; PF19305; MmgE_PrpD_C; 1.
DR   SUPFAM; SSF103378; SSF103378; 1.
PE   1: Evidence at protein level;
KW   Lyase; Tricarboxylic acid cycle.
FT   CHAIN           1..505
FT                   /note="2-methylcitrate dehydratase"
FT                   /id="PRO_0000432934"
SQ   SEQUENCE   505 AA;  55157 MW;  B5C5A45A74B46322 CRC64;
     MVRIMLMHAV RAWRSADDFP CTEHMAYKIA QVAADPVDVD PEVADMVCNR IIDNAAVSAA
     SMVRRPVTVA RHQALAHPVR HGAKVFGVEG SYSADWAAWA NGVAARELDF HDTFLAADYS
     HPADNIPPLV AVAQQLGVCG AELIRGLVTA YEIHIDLTRG ICLHEHKIDH VAHLGPAVAA
     GIGTMLRLDQ ETIYHAIGQA LHLTTSTRQS RKGAISSWKA FAPAHAGKVG IEAVDRAMRG
     EGSPAPIWEG EDGVIAWLLA GPEHTYRVPL PAPGEPKRAI LDSYTKQHSA EYQSQAPIDL
     ACRLRERIGD LDQIASIVLH TSHHTHVVIG TGSGDPQKFD PDASRETLDH SLPYIFAVAL
     QDGCWHHERS YAPERARRSD TVALWHKIST VEDPEWTRRY HCADPAKKAF GARAEVTLHS
     GEVIVDELAV ADAHPLGTRP FERKQYVEKF TELADGVVEP VEQQRFLAVV ESLADLESGA
     VGGLNVLVDP RVLDKAPVIP PGIFR