PRPD_SALTI
ID PRPD_SALTI Reviewed; 483 AA.
AC Q8Z903;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=2-methylcitrate dehydratase {ECO:0000250|UniProtKB:P74840};
DE Short=2-MC dehydratase {ECO:0000250|UniProtKB:P74840};
DE EC=4.2.1.79 {ECO:0000250|UniProtKB:P74840};
DE AltName: Full=Aconitate hydratase {ECO:0000250|UniProtKB:P74840};
DE Short=ACN {ECO:0000250|UniProtKB:P74840};
DE Short=Aconitase {ECO:0000250|UniProtKB:P74840};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:P74840};
GN Name=prpD; OrderedLocusNames=STY0402, t2494;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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:P74840}.
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:P74840};
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:P74840};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000250|UniProtKB:P74840}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:P74840}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P77243}.
CC -!- SIMILARITY: Belongs to the PrpD family. {ECO:0000305}.
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DR EMBL; AL513382; CAD08825.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70082.1; -; Genomic_DNA.
DR RefSeq; NP_454965.1; NC_003198.1.
DR RefSeq; WP_001272709.1; NZ_CJUM01000013.1.
DR PDB; 5MVI; X-ray; 3.05 A; A/B/C/D/E/F=1-483.
DR PDBsum; 5MVI; -.
DR AlphaFoldDB; Q8Z903; -.
DR SMR; Q8Z903; -.
DR STRING; 220341.16501639; -.
DR EnsemblBacteria; AAO70082; AAO70082; t2494.
DR KEGG; stt:t2494; -.
DR KEGG; sty:STY0402; -.
DR PATRIC; fig|220341.7.peg.398; -.
DR eggNOG; COG2079; Bacteria.
DR HOGENOM; CLU_021803_1_0_6; -.
DR OMA; ECTKHLG; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
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:0019629; P:propionate catabolic process, 2-methylcitrate cycle; ISS: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 3D-structure; Lyase; Tricarboxylic acid cycle.
FT CHAIN 1..483
FT /note="2-methylcitrate dehydratase"
FT /id="PRO_0000215025"
FT CONFLICT 452
FT /note="L -> P (in Ref. 2; AAO70082)"
FT /evidence="ECO:0000305"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 31..51
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:5MVI"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 141..159
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 173..186
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 220..239
FT /evidence="ECO:0007829|PDB:5MVI"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:5MVI"
FT TURN 247..251
FT /evidence="ECO:0007829|PDB:5MVI"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:5MVI"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:5MVI"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:5MVI"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 374..379
FT /evidence="ECO:0007829|PDB:5MVI"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 389..396
FT /evidence="ECO:0007829|PDB:5MVI"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:5MVI"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:5MVI"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 432..448
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 453..463
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 466..469
FT /evidence="ECO:0007829|PDB:5MVI"
FT HELIX 474..479
FT /evidence="ECO:0007829|PDB:5MVI"
SQ SEQUENCE 483 AA; 53770 MW; 4C695F381E7E228A CRC64;
MSAHISNVRP DFDREIVDIV DYVMNYEITS KVAYDTAHYC LLDTLGCGLE ALEYPACKKL
LGPIVPGTVV PNGARVPGTQ FQLDPVQAAF NISAMIRWLD 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 FLTRQQQRIL DVSLDRARLE QMPVNEYLDL
YII
