(data stored in ACNUC7421 zone)

SWISSPROT: 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   05-JUL-2017, entry version 94.
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=(2S,3S)-2-methylcitrate dehydratase {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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and 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
CC       (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route)
CC       and via the 2-methylcitrate cycle I (propionate degradation
CC       route). Catalyzes the stereospecific dehydration of (2S,3S)-2-
CC       methylcitrate (2-MC) to yield the cis isomer of 2-methyl-
CC       aconitate. Could also catalyze the dehydration of citrate and the
CC       hydration of cis-aconitate. {ECO:0000250|UniProtKB:P77243}.
CC   -!- CATALYTIC ACTIVITY: (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate =
CC       (Z)-but-2-ene-1,2,3-tricarboxylate + H(2)O.
CC       {ECO:0000250|UniProtKB:P77243}.
CC   -!- CATALYTIC ACTIVITY: Citrate = isocitrate.
CC       {ECO:0000250|UniProtKB:P77243}.
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000250|UniProtKB:P77243}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       isocitrate from oxaloacetate: step 2/2.
CC       {ECO:0000250|UniProtKB:P77243}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P77243}.
CC   -!- SIMILARITY: Belongs to the PrpD family. {ECO:0000305}.
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_MWVM01000022.1.
DR   ProteinModelPortal; Q8X693; -.
DR   SMR; Q8X693; -.
DR   STRING; 155864.Z0429; -.
DR   EnsemblBacteria; AAG54682; AAG54682; Z0429.
DR   EnsemblBacteria; BAB33810; BAB33810; BAB33810.
DR   GeneID; 914489; -.
DR   KEGG; ece:Z0429; -.
DR   KEGG; ecs:ECs0387; -.
DR   PATRIC; fig|386585.9.peg.482; -.
DR   eggNOG; ENOG4105DXD; Bacteria.
DR   eggNOG; COG2079; LUCA.
DR   HOGENOM; HOG000159916; -.
DR   KO; K01720; -.
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:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:InterPro.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR012705; 2Me_IsoCit_deHydtase_PrpD.
DR   InterPro; IPR005656; MmgE_PrpD.
DR   PANTHER; PTHR16943; PTHR16943; 1.
DR   Pfam; PF03972; MmgE_PrpD; 1.
DR   SUPFAM; SSF103378; SSF103378; 1.
DR   TIGRFAMs; TIGR02330; prpD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X693.
DR   SWISS-2DPAGE; Q8X693.
KW   Complete proteome; Lyase; Tricarboxylic acid cycle.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    483       2-methylcitrate dehydratase.
FT                                /FTId=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
//

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