PRPC1_CORGL
ID PRPC1_CORGL Reviewed; 381 AA.
AC Q8NSH7;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=2-methylcitrate synthase 1 {ECO:0000303|PubMed:11976302};
DE Short=2-MCS {ECO:0000303|PubMed:11976302};
DE Short=MCS {ECO:0000303|PubMed:11976302};
DE EC=2.3.3.5 {ECO:0000269|PubMed:11976302};
DE AltName: Full=Citrate synthase 1 {ECO:0000303|PubMed:11976302};
DE Short=CS {ECO:0000303|PubMed:11976302};
DE EC=2.3.3.16 {ECO:0000269|PubMed:11976302};
GN Name=prpC1; OrderedLocusNames=Cgl0696, cg0798;
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, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, 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: Catalyzes the Claisen condensation of propionyl-CoA and
CC oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also
CC catalyzes the condensation of oxaloacetate with propionyl-CoA but with
CC a lower specificity. {ECO:0000269|PubMed:11976302}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-methylcitrate +
CC CoA + H(+); Xref=Rhea:RHEA:23780, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:58853; EC=2.3.3.5;
CC Evidence={ECO:0000269|PubMed:11976302};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.16;
CC Evidence={ECO:0000269|PubMed:11976302};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC {ECO:0000305|PubMed:11976302}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P31660}.
CC -!- INDUCTION: By propionate. {ECO:0000269|PubMed:11976302}.
CC -!- MISCELLANEOUS: The prpD1B1C1 operon seems not to be involved in
CC propionate degradation. {ECO:0000269|PubMed:11976302}.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB98089.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF434798; AAM21502.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98089.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927150; CAF19401.1; -; Genomic_DNA.
DR RefSeq; NP_599928.1; NC_003450.3.
DR RefSeq; WP_011013823.1; NC_006958.1.
DR AlphaFoldDB; Q8NSH7; -.
DR SMR; Q8NSH7; -.
DR STRING; 196627.cg0798; -.
DR KEGG; cgb:cg0798; -.
DR KEGG; cgl:Cgl0696; -.
DR PATRIC; fig|196627.13.peg.682; -.
DR eggNOG; COG0372; Bacteria.
DR HOGENOM; CLU_025068_2_1_11; -.
DR OMA; HADHEMN; -.
DR BRENDA; 2.3.3.5; 960.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:UniProtKB.
DR GO; GO:0036440; F:citrate synthase activity; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR019810; Citrate_synthase_AS.
DR InterPro; IPR024176; Citrate_synthase_bac-typ.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01800; cit_synth_II; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..381
FT /note="2-methylcitrate synthase 1"
FT /id="PRO_0000169979"
FT ACT_SITE 227
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 266
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 317
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 260..264
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
SQ SEQUENCE 381 AA; 42567 MW; 9C69BC244B431B20 CRC64;
MSDSQVRKGL NGVISDYTSI SKVMPESNSL TYRGYAVEDL VENCSFEEVI YLLWFGELPT
TEQLRTFNTT GRSYRSLDAG LISLIHSLPN TCHPMDVLRT AVSYMGTFDP DPFTRDADHI
RSIGHNLLAQ LPMVVAMDIR RRSGEEIIAP DHNKGIASNF LSMVFGNDDG SVANSADDIR
DFERSLILYA EHSFNASTFS ARVISSTRSD TYSAITGAIG ALKGPLHGGA NEFVMHTMLD
IDDPNNAADW MGKALDRKER IMGFGHRVYK NGDSRVPSME KSMRSLAARH RGQKWVHMYE
SMQEVMEART GIKPNLDFPA GPAYYMLGFP VDFFTPLFVL ARVSGWTAHI VEQFENNALI
RPLSAYNGVE EREVVPISER T
