PRPD_SALTY
ID PRPD_SALTY Reviewed; 483 AA.
AC P74840;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=2-methylcitrate dehydratase {ECO:0000303|PubMed:11294638};
DE Short=2-MC dehydratase {ECO:0000303|PubMed:11294638};
DE EC=4.2.1.79 {ECO:0000269|PubMed:11294638};
DE AltName: Full=Aconitate hydratase {ECO:0000303|PubMed:11294638};
DE Short=ACN {ECO:0000303|PubMed:11294638};
DE Short=Aconitase {ECO:0000303|PubMed:11294638};
DE EC=4.2.1.3 {ECO:0000269|PubMed:11294638};
GN Name=prpD; OrderedLocusNames=STM0370;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=9006051; DOI=10.1128/jb.179.3.928-940.1997;
RA Horswill A.R., Escalante-Semerena J.C.;
RT "Propionate catabolism in Salmonella typhimurium LT2: two divergently
RT transcribed units comprise the prp locus at 8.5 centisomes, prpR encodes a
RT member of the sigma-54 family of activators, and the prpBCDE genes
RT constitute an operon.";
RL J. Bacteriol. 179:928-940(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=10482501; DOI=10.1128/jb.181.18.5615-5623.1999;
RA Horswill A.R., Escalante-Semerena J.C.;
RT "Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric
RT acid cycle.";
RL J. Bacteriol. 181:5615-5623(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=LT2;
RX PubMed=11294638; DOI=10.1021/bi015503b;
RA Horswill A.R., Escalante-Semerena J.C.;
RT "In vitro conversion of propionate to pyruvate by Salmonella enterica
RT enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase enzymes catalyze
RT the conversion of 2-methylcitrate to 2-methylisocitrate.";
RL Biochemistry 40:4703-4713(2001).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the 2-methylcitrate cycle I (propionate degradation route).
CC Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield the cis
CC isomer of 2-methyl-aconitate. It is also able to catalyze the
CC dehydration of citrate at a lower rate, and the hydration of cis-
CC aconitate. It has no aconitase-like activity and is unable to catalyze
CC the hydration of 2-methyl-cis-aconitate. {ECO:0000269|PubMed:10482501,
CC ECO:0000269|PubMed:11294638}.
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:0000269|PubMed:11294638};
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:0000269|PubMed:11294638};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305|PubMed:9006051}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000305|PubMed:11294638}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P77243}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate 2-
CC methylcitrate during growth on propionate.
CC {ECO:0000269|PubMed:10482501}.
CC -!- SIMILARITY: Belongs to the PrpD family. {ECO:0000305}.
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DR EMBL; U51879; AAC44816.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19324.1; -; Genomic_DNA.
DR RefSeq; NP_459365.1; NC_003197.2.
DR RefSeq; WP_000107071.1; NC_003197.2.
DR AlphaFoldDB; P74840; -.
DR SMR; P74840; -.
DR STRING; 99287.STM0370; -.
DR PaxDb; P74840; -.
DR EnsemblBacteria; AAL19324; AAL19324; STM0370.
DR GeneID; 1251889; -.
DR KEGG; stm:STM0370; -.
DR PATRIC; fig|99287.12.peg.392; -.
DR HOGENOM; CLU_021803_1_0_6; -.
DR OMA; ECTKHLG; -.
DR PhylomeDB; P74840; -.
DR BioCyc; MetaCyc:MON-64; -.
DR BioCyc; SENT99287:STM0370-MON; -.
DR BRENDA; 4.2.1.79; 2169.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000001014; Chromosome.
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:0019543; P:propionate catabolic process; IGI:SGD.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IDA:UniProtKB.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
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 1: Evidence at protein level;
KW Lyase; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..483
FT /note="2-methylcitrate dehydratase"
FT /id="PRO_0000215026"
FT CONFLICT 308
FT /note="Q -> H (in Ref. 1; AAC44816)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 53787 MW; CF045F6958157467 CRC64;
MSTQELNIRP DFDREIVDIV DYVMNYEITS KVAYDTAHYC LLDTLGCGLE ALEYPACKKL
LGPIVPGTVV PNGARVPGTQ FQLDPVQAAF NIGAMIRWLD FNDTWLAAEW GHPSDNLGGI
LATADWLSRN AVAAGKAPLT MKQVLSGMIK AHEIQGCIAL ENAFNRVGLD HVLLVKVAST
AVVAEMLGLT RDEILNAVSL AWVDGQSLRT YRHAPNTGTR KSWAAGDATS RAVRLALMAK
TGEMGYPSAL TAKTWGFYDV SFKGETFRFQ RPYGSYVMEN VLFKISFPAE FHSQTAVEAA
MTLYEQMQAA GKTAADIEKV TIRTHEACLR IIDKKGPLNN PADRDHCIQY MVAVPLLFGR
LTAADYEDEV AQDKRIDALR EKIVCYEDPA FTADYHDPEK RAIGNAITVE FTDGSRFGEV
VVEYPIGHAR RRADGIPKLI EKFKINLARQ FPTRQQQRIL DVSLDRARLE QMPVNEYLDL
YVI
