ID   PRPD_CUPNE              Reviewed;         484 AA.
AC   Q937N6;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=2-methylcitrate dehydratase {ECO:0000303|PubMed:11495997};
DE            Short=2-MC dehydratase {ECO:0000303|PubMed:11495997};
DE            EC=4.2.1.79 {ECO:0000250|UniProtKB:P77243};
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   Name=prpD;
OS   Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=106590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=HF39;
RX   PubMed=11495997; DOI=10.1099/00221287-147-8-2203;
RA   Bramer C.O., Steinbuchel A.;
RT   "The methylcitric acid pathway in Ralstonia eutropha: new genes identified
RT   involved in propionate metabolism.";
RL   Microbiology 147:2203-2214(2001).
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:11495997). Could also catalyze the dehydration
CC       of citrate and the hydration of cis-aconitate (By similarity).
CC       {ECO:0000250|UniProtKB:P77243, ECO:0000269|PubMed:11495997}.
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:0000250|UniProtKB:P77243};
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:11495997}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 2/2. {ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P77243}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are still able to use
CC       propionate as carbon source. {ECO:0000269|PubMed:11495997}.
CC   -!- SIMILARITY: Belongs to the PrpD family. {ECO:0000305}.
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DR   EMBL; AF325554; AAL03992.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q937N6; -.
DR   SMR; Q937N6; -.
DR   PRIDE; Q937N6; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
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; TAS: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; IPR012705; 2Me_IsoCit_deHydtase_PrpD.
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.
DR   TIGRFAMs; TIGR02330; prpD; 1.
PE   3: Inferred from homology;
KW   Lyase; Tricarboxylic acid cycle.
FT   CHAIN           1..484
FT                   /note="2-methylcitrate dehydratase"
FT                   /id="PRO_0000432933"
SQ   SEQUENCE   484 AA;  53002 MW;  21B5C1A44031E212 CRC64;
     MSTDTPSAQR PDPDQVLVDI VDYVTRYEIK SGLAYDTARN CLIDTLGCGL EALSYPACTK
     LLGPVVPGTI VPNGARVPGT QFQLDPVQAA FNIGAMIRWL DFNDTWLAAE WGHPSDNLGG
     ILATADWISR NHIAAGRKPL TMKAVLAAMI KAHEIQGCIA LENSFNQVGL DHVVLVKVAS
     TAVVAQMLGL TRDEILNAVS LAWVDGQSLR TYRHAPNAGS RKSWAHGDAT SRAVRLALIA
     RTGEMGYPSV LTAKTWGFYD VLFKGQPFRF QRPYGTYVME NILLKISYPA EFHAQTAVEA
     AMQLHGALAL AGRSAADIAA ITIRTHEACL RIIDKLGPLS NPADRDHCIQ YMVAVPLLFG
     RLTAADYEDR IAADPRIDAL RGRITCVEDP ALTRDYHDPA KRSIANALTV TLADGTVLDE
     VLVEYPLGHK RRRAEGIPLL VEKFRTNLAR RFPPKQQQAI LAASLDQARL EAMPVNEYLD
     MYAI