PRPC2_CORGL
ID PRPC2_CORGL Reviewed; 383 AA.
AC Q8NSL1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=2-methylcitrate synthase 2 {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 2 {ECO:0000303|PubMed:11976302};
DE Short=CS {ECO:0000303|PubMed:11976302};
DE EC=2.3.3.16 {ECO:0000269|PubMed:11976302};
GN Name=prpC2; OrderedLocusNames=Cgl0659, cg0762;
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: 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 Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield
CC 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of
CC oxaloacetate with acetyl-CoA but with a lower specificity.
CC {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: 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|PubMed:11976302}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P31660}.
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 citrate synthase family. {ECO:0000305}.
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DR EMBL; AF434799; AAM21506.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98052.1; -; Genomic_DNA.
DR EMBL; BX927149; CAF19365.1; -; Genomic_DNA.
DR RefSeq; NP_599891.1; NC_003450.3.
DR RefSeq; WP_011013797.1; NC_006958.1.
DR AlphaFoldDB; Q8NSL1; -.
DR SMR; Q8NSL1; -.
DR STRING; 196627.cg0762; -.
DR KEGG; cgb:cg0762; -.
DR KEGG; cgl:Cgl0659; -.
DR PATRIC; fig|196627.13.peg.645; -.
DR eggNOG; COG0372; Bacteria.
DR HOGENOM; CLU_025068_2_1_11; -.
DR OMA; NEAVMHM; -.
DR BRENDA; 2.3.3.5; 960.
DR UniPathway; UPA00223; UER00717.
DR UniPathway; UPA00946; -.
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:0019679; P:propionate metabolic process, methylcitrate cycle; 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..383
FT /note="2-methylcitrate synthase 2"
FT /id="PRO_0000169980"
FT ACT_SITE 230
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 269
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 320
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 263..267
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
SQ SEQUENCE 383 AA; 42595 MW; FD298103E073E178 CRC64;
MSSATTTDVR KGLYGVIADY TAVSKVMPET NSLTYRGYAV EDLVENCSFE EVFYLLWHGE
LPTAQQLAEF NERGRSYRSL DAGLISLIHS LPKEAHPMDV MRTAVSYMGT KDSEYFTTDS
EHIRKVGHTL LAQLPMVLAM DIRRRKGLDI IAPDSSKSVA ENLLSMVFGT GPESPASNPA
DVRDFEKSLI LYAEHSFNAS TFTARVITST KSDVYSAITG AIGALKGPLH GGANEFVMHT
MLAIDDPNKA AAWINNALDN KNVVMGFGHR VYKRGDSRVP SMEKSFRELA ARHDGEKWVA
MYENMRDAMD ARTGIKPNLD FPAGPAYHLL GFPVDFFTPL FVIARVAGWT AHIVEQYENN
SLIRPLSEYN GEEQREVAPI EKR
