PRPD1_CORGL
ID PRPD1_CORGL Reviewed; 498 AA.
AC Q8NSH9;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=2-methylcitrate dehydratase 1 {ECO:0000303|PubMed:11976302};
DE Short=2-MC dehydratase {ECO:0000303|PubMed:11976302};
DE EC=4.2.1.79 {ECO:0000250|UniProtKB:P77243};
GN Name=prpD1; OrderedLocusNames=Cgl0694, cg0796;
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], AND FUNCTION.
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: Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield
CC the cis isomer 2-methyl-aconitate. {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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P77243}.
CC -!- MISCELLANEOUS: The prpD1B1C1 operon seems not to be involved in
CC propionate degradation. {ECO:0000269|PubMed:11976302}.
CC -!- SIMILARITY: Belongs to the PrpD family. {ECO:0000305}.
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DR EMBL; AF434798; AAM21500.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98087.1; -; Genomic_DNA.
DR EMBL; BX927150; CAF19399.1; -; Genomic_DNA.
DR RefSeq; NP_599926.1; NC_003450.3.
DR RefSeq; WP_011013821.1; NC_006958.1.
DR AlphaFoldDB; Q8NSH9; -.
DR SMR; Q8NSH9; -.
DR STRING; 196627.cg0796; -.
DR KEGG; cgb:cg0796; -.
DR KEGG; cgl:Cgl0694; -.
DR PATRIC; fig|196627.13.peg.680; -.
DR eggNOG; COG2079; Bacteria.
DR HOGENOM; CLU_026574_3_0_11; -.
DR OMA; RDHCLRY; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0047547; F:2-methylcitrate dehydratase activity; IDA:UniProtKB.
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 3: Inferred from homology;
KW Lyase; Reference proteome.
FT CHAIN 1..498
FT /note="2-methylcitrate dehydratase 1"
FT /id="PRO_0000215021"
SQ SEQUENCE 498 AA; 55013 MW; 626F96A36B9227C3 CRC64;
MRIHDVYTHL SADNFPKAEH LAWKFSELAT DPVEVTPDVS EMIINRIIDN AAVSAASVLR
RPVTVARQQA QSHPREKGGK VFGISGSYSP EWAAFANGVA VRELDFHDTF LAAEYSHPGD
NIPPLLAVAQ AQRSSGRDLI RGIATAYEVQ VELVRGICLH EHKIDHVAHL GPSAAAGLGT
LLHVDEETIY QAIGQALHTT TATRQSRKGE ISSWKAFAPA FAGKMAIEAM DRAMRGEGSP
APIWEGEDGV IAWLLSGKDH VYHVPLPEHG EPKLGILETY TKEHSAEYQS QAPIDLARRM
KPLVDAAGGT EHIAEIVLRT SHHTHYVIGT GANDPQKMDP QASRETLDHS IMYIFAVALQ
DGVWHHEFSY TRKRSTRPET VELWHKIRTV EDPEWTRRYH SDDPAKKAFG AKAVITMADG
TVIEDELAVA DAHPLGARPF ARENYIEKFR TLAQGIVIDS EQERFLHAVQ SLPDLDDLDQ
LNIEVDISNQ AATKAGLL