ID PRPD_ECO57 Reviewed; 483 AA. AC Q8X693; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 122. DE RecName: Full=2-methylcitrate dehydratase {ECO:0000250|UniProtKB:P77243}; DE Short=2-MC dehydratase {ECO:0000250|UniProtKB:P77243}; DE EC=4.2.1.79 {ECO:0000250|UniProtKB:P77243}; DE AltName: Full=Probable 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; OrderedLocusNames=Z0429, ECs0387; OS Escherichia coli O157:H7. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(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. Could also catalyze the dehydration of citrate and CC the hydration of cis-aconitate. {ECO:0000250|UniProtKB:P77243}. 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:0000250|UniProtKB:P77243}. CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate CC from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:P77243}. CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P77243}. CC -!- SIMILARITY: Belongs to the PrpD family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE005174; AAG54682.1; -; Genomic_DNA. DR EMBL; BA000007; BAB33810.1; -; Genomic_DNA. DR PIR; C90677; C90677. DR PIR; F85527; F85527. DR RefSeq; NP_308414.1; NC_002695.1. DR RefSeq; WP_001275870.1; NZ_VOAI01000005.1. DR AlphaFoldDB; Q8X693; -. DR SMR; Q8X693; -. DR STRING; 155864.Z0429; -. DR GeneID; 914489; -. DR KEGG; ece:Z0429; -. DR KEGG; ecs:ECs_0387; -. DR PATRIC; fig|386585.9.peg.482; -. DR eggNOG; COG2079; Bacteria. DR HOGENOM; CLU_021803_1_0_6; -. DR OMA; DHSVMYI; -. DR UniPathway; UPA00223; UER00718. DR UniPathway; UPA00946; -. DR Proteomes; UP000000558; Chromosome. DR Proteomes; UP000002519; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0047547; F:2-methylcitrate dehydratase activity; ISS:UniProtKB. DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; ISS:UniProtKB. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.4100.10; 2-methylcitrate dehydratase PrpD; 1. DR Gene3D; 3.30.1330.120; 2-methylcitrate dehydratase PrpD; 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 NCBIfam; TIGR02330; prpD; 1. DR PANTHER; PTHR16943; 2-METHYLCITRATE DEHYDRATASE-RELATED; 1. DR PANTHER; PTHR16943:SF8; 2-METHYLCITRATE DEHYDRATASE-RELATED; 1. DR Pfam; PF19305; MmgE_PrpD_C; 1. DR Pfam; PF03972; MmgE_PrpD_N; 1. DR SUPFAM; SSF103378; 2-methylcitrate dehydratase PrpD; 1. PE 3: Inferred from homology; KW Lyase; Reference proteome; Tricarboxylic acid cycle. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..483 FT /note="2-methylcitrate dehydratase" FT /id="PRO_0000215024" SQ SEQUENCE 483 AA; 53952 MW; 288942C490E56F86 CRC64; MSAQINNIRP EFDREIVDIV DYVMNYEISS KVAYDTAHYC LLDTLGCGLE ALEYPACKKL LGPIVPGTVV PNGVRVPGTQ FQLDPVQAAF NIGAMIRWLD FNDTWLAAEW GHPSDNLGGI LATADWLSRN AVASGKAPLT MKQVLTGMIK AHEIQGCIAL ENSFNRVGLD HVLLVKVAST AVVAEMLGLT REEILNAVSL AWVDGQSLRT YRHAPNTGTR KSWAAGDATS RAVRLALMAK TGEMGYPSAL TAPVWGFYDV SFKGESFRFQ RPYGSYVMEN VLFKISFPAE FHSQTAVEAA MTLYEQMQAA GKTAADIEKV SIRTHEACIR IIDKKGPLNN PADRDHCIQY MVAIPLLFGR LTAADYEDNV AQDKRIDALR EKINCFEDPV FTADYHDPEK RAIANAITLE FTDGTRFEEV VVEYPIGHAR RRQDGIPKLV DKFKINLARQ FPTRQQQRIL EVSLDRARLE QMPVNEYLDL YVI //