PRPD2_CORGL
ID PRPD2_CORGL Reviewed; 504 AA.
AC Q8NSL3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=2-methylcitrate dehydratase 2 {ECO:0000303|PubMed:11976302};
DE Short=2-MC dehydratase {ECO:0000303|PubMed:11976302};
DE EC=4.2.1.79 {ECO:0000250|UniProtKB:P77243};
DE AltName: Full=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=prpD2; OrderedLocusNames=Cgl0657, cg0759;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=11976302; DOI=10.1128/jb.184.10.2728-2739.2002;
RA Claes W.A., Puehler A., Kalinowski J.;
RT "Identification of two prpDBC gene clusters in Corynebacterium glutamicum
RT and their involvement in propionate degradation via the 2-methylcitrate
RT cycle.";
RL J. Bacteriol. 184:2728-2739(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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 2-methyl-aconitate (PubMed:11976302). Could also catalyze the
CC dehydration of citrate and the hydration of cis-aconitate (By
CC similarity). {ECO:0000250|UniProtKB:P77243,
CC ECO:0000269|PubMed:11976302}.
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:0000305|PubMed:11976302}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P77243}.
CC -!- INDUCTION: By propionate. {ECO:0000269|PubMed:11976302}.
CC -!- MISCELLANEOUS: The prpD2B2C2 operon is essential for growth on
CC propionate as sole carbon source. {ECO:0000269|PubMed:11976302}.
CC -!- SIMILARITY: Belongs to the PrpD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB98050.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF434799; AAM21504.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98050.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BX927149; CAF19363.1; -; Genomic_DNA.
DR RefSeq; WP_011265602.1; NC_006958.1.
DR AlphaFoldDB; Q8NSL3; -.
DR SMR; Q8NSL3; -.
DR STRING; 196627.cg0759; -.
DR KEGG; cgb:cg0759; -.
DR KEGG; cgl:Cgl0657; -.
DR eggNOG; COG2079; Bacteria.
DR HOGENOM; CLU_087220_0_0_11; -.
DR OMA; ECTKHLG; -.
DR UniPathway; UPA00223; UER00717.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000582; Chromosome.
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:0019679; P:propionate metabolic process, methylcitrate cycle; IDA: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; 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.
PE 2: Evidence at transcript level;
KW Lyase; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..504
FT /note="2-methylcitrate dehydratase 2"
FT /id="PRO_0000215022"
SQ SEQUENCE 504 AA; 55396 MW; 12B6DFF430DD9D3B CRC64;
MINHEVRTHR SAEEFPYEEH LAHKIARVAA DPVEVAADTQ EMIINRIIDN ASVQAASVLR
RPVSSARAMA QVRPVTDGRG ASVFGLPGRY AAEWAALANG TAVRELDFHD TFLAAEYSHP
GDNIPPILAA AQQAGKGGKD LIRGIATGYE IQVNLVRGMC LHEHKIDHVA HLGPSAAAGI
GTLLDLDVDT IYQAIGQALH TTTATRQSRK GAISSWKAFA PAFAGKMSIE AVDRAMRGEG
APSPIWEGED GVIAWLLSGL DHIYTIPLPA EGEAKRAILD TYTKEHSAEY QSQAPIDLAR
SMGEKLAAQG LDLRDVDSIV LHTSHHTHYV IGTGSNDPQK FDPDASRETL DHSIMYIFAV
ALEDRAWHHE RSYAPERAHR RETIELWNKI STVEDPEWTR RYHSVDPAEK AFGARAVITF
KDGTVVEDEL AVADAHPLGA RPFAREQYIQ KFRTLAEGVV SEKEQDRFLD AAQRTHELED
LSELNIELDA DILAKAPVIP EGLF
