PRPD_ECO57
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 03-AUG-2022, entry version 114.
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; Proteobacteria; 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}.
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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_SWKA01000005.1.
DR AlphaFoldDB; Q8X693; -.
DR SMR; Q8X693; -.
DR STRING; 155864.EDL933_0392; -.
DR EnsemblBacteria; AAG54682; AAG54682; Z0429.
DR EnsemblBacteria; BAB33810; BAB33810; ECs_0387.
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; ECTKHLG; -.
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:0047780; F:citrate dehydratase 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; -; 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; 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
