ID   A9IIR3_BORPD            Unreviewed;       483 AA.
AC   A9IIR3;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   02-SEP-2026, entry version 79.
DE   RecName: Full=2-methylcitrate dehydratase {ECO:0000256|ARBA:ARBA00017240};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.79 {ECO:0000256|ARBA:ARBA00013124};
GN   Name=prpD {ECO:0000313|EMBL:CAP42151.1};
GN   OrderedLocusNames=Bpet1812 {ECO:0000313|EMBL:CAP42151.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448 / CIP
OS   107267 / Se-1111R).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42151.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP42151.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448 / CIP 107267 / Se-1111R
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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:0000256|ARBA:ARBA00000096};
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:0000256|ARBA:ARBA00023501};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000256|ARBA:ARBA00005026}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the PrpD family.
CC       {ECO:0000256|ARBA:ARBA00006174}.
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DR   EMBL; AM902716; CAP42151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IIR3; -.
DR   STRING; 94624.Bpet1812; -.
DR   KEGG; bpt:Bpet1812; -.
DR   eggNOG; COG2079; Bacteria.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000001225; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0047547; F:2-methylcitrate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019541; P:propionate metabolic process; IEA:UniProtKB-ARBA.
DR   FunFam; 1.10.4100.10:FF:000001; 2-methylcitrate dehydratase; 1.
DR   FunFam; 3.30.1330.120:FF:000001; 2-methylcitrate dehydratase; 1.
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; NF006943; PRK09425.1; 1.
DR   NCBIfam; TIGR02330; prpD; 1.
DR   PANTHER; PTHR16943:SF8; 2-METHYLCITRATE DEHYDRATASE; 1.
DR   PANTHER; PTHR16943; 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 {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CAP42151.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001225};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          18..270
FT                   /note="MmgE/PrpD N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03972"
FT   DOMAIN          287..465
FT                   /note="MmgE/PrpD C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19305"
SQ   SEQUENCE   483 AA;  53559 MW;  209BF87B68AD5208 CRC64;
     MSTPVSNIRP EPDQVLVDIV DYVLGYEIDS KLAYETARNC LIDTLGCGLE ALEYPACRKL
     LGPIVPGTVV PNGAKVPGTQ FQLDPVQAAF NIGAMIRWLD FNDTWLAAEW GHPSDNLGGI
     LATADWLSRN AIAAGKAPLT MRDVLAGMIK AHEIQGCIAL ENSFNKVGLD HVVLVKVATT
     AVVAQLLGLD REETINAVSL AWVDGQSLRT YRHAPNTGSR KSWAAGDATS RAVRLALMAR
     TGEMGYPSVL TTKTWGFYDV LFKGQPFKFQ RPYGSYVMEN VLFKISFPAE FHAQTAVECA
     MDIHKRLQAA GKSAGDISRI TIRTHEACIR IIDKKGPRNN PADRDHCIQY MVAVPVLFGR
     LTAADYEDDV ARDPRIDALR DKIVCVEDPA FTRDYHDPDK RSIANALTVE FNDGTRLDEI
     VCEYPIGHKR RRQEGIPLLE AKFRTNLARI FPPRQQARIL AASLDQQTLE AMPVHEYVDL
     YVI
//