2-methylcitrate synthase (P31660)

Identification
Name:2-methylcitrate synthase
Synonyms:
  • Citrate synthase 2
  • Methylcitrate synthase
Gene Name:prpC
Enzyme Class:
Biological Properties
General Function:Involved in transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Specific Function:Catalyzes the synthesis of 2-methylcitrate from propionyl-CoA and oxaloacetate. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0Oxalacetic acid + 1.0Propionyl-CoA ↔ 1.0Methylcitric acid + 1.0Coenzyme A + 1.0Hydrogen ion + 1.0(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Methylcitric acid + 1.0Coenzyme A ↔ 1.0Propionyl-CoA + 1.0Oxalacetic acid + 1.0Water
ReactionCard
SMPDB Reactions:
1.0Propionyl-CoA+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.02-Methylcitric acid+1.0Thumb
1.0Propionyl-CoA + 1.0Water + 1.0Oxalacetic acid + 1.0Propionyl-CoA → 1.0Coenzyme A + 1.0Hydrogen ion + 1.02-Methylcitric acid + 1.0Methylcitric acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0Oxalacetic acid + 1.0Propionyl-CoA ↔ 1.0Methylcitric acid + 1.0Coenzyme A + 1.0Hydrogen ion + 1.0(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB23052(2R,3S)-2-Hydroxybutane-1,2,3-tricarboxylateMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00723Methylcitric acidMetaboCard
ECMDB00223Oxalacetic acidMetaboCard
ECMDB01275Propionyl-CoAMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Process
acetyl-CoA catabolic process
acetyl-CoA metabolic process
carbohydrate metabolic process
cellular carbohydrate metabolic process
cellular metabolic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
primary metabolic process
tricarboxylic acid cycle
Gene Properties
Blattner:b0333
Gene OrientationClockwise
Centisome Percentage:7.53
Left Sequence End349236
Right Sequence End350405
Gene Sequence:
>1170 bp
ATGAGCGACACAACGATCCTGCAAAACAGTACCCATGTCATTAAACCGAAAAAATCTGTG
GCACTTTCTGGCGTTCCGGCGGGCAATACGGCGCTCTGCACCGTGGGTAAAAGTGGCAAT
GACCTGCATTACCGCGGCTACGATATTCTTGATCTGGCGAAACATTGCGAATTTGAAGAA
GTGGCGCATCTGCTGATCCACGGCAAACTGCCGACCCGTGACGAACTCGCCGCTTACAAA
ACGAAACTGAAAGCCCTGCGCGGTTTACCGGCTAACGTGCGTACCGTGCTGGAAGCCTTA
CCGGCGGCGTCGCACCCGATGGATGTTATGCGCACCGGTGTTTCCGCGCTCGGCTGCACG
CTGCCAGAAAAAGAGGGGCATACCGTCTCTGGCGCGCGGGATATTGCCGACAAACTGCTG
GCGTCGCTTAGCTCGATTCTCCTTTATTGGTATCACTACAGCCACAACGGCGAACGCATC
CAACCGGAAACCGATGACGACTCCATCGGCGGTCACTTCCTGCATCTGCTGCACGGCGAA
AAGCCATCGCAAAGCTGGGAAAAGGCGATGCATATCTCGCTGGTGCTGTACGCCGAACAC
GAGTTTAACGCCTCCACCTTTACCAGTCGGGTGATTGCGGGCACCGGCTCTGATATGTAT
TCCGCGATTATTGGCGCGATTGGCGCACTGCGCGGGCCAAAACACGGCGGGGCGAATGAA
GTGTCGCTGGAGATCCAGCAACGCTACGAAACGCCGGACGAAGCCGAAGCAGATATCCGC
AAGCGCGTGGAAAACAAAGAAGTGGTCATTGGTTTTGGTCATCCGGTTTACACCATCGCT
GACCCGCGCCACCAGGTGATTAAACGTGTGGCGAAGCAGCTCTCGCAGGAAGGCGGCTCG
CTGAAGATGTACAACATCGCCGATCGCCTGGAAACGGTGATGTGGGAGAGCAAAAAGATG
TTCCCCAATCTCGACTGGTTCTCTGCTGTTTCCTACAACATGATGGGCGTTCCCACCGAG
ATGTTCACACCACTGTTTGTTATCGCCCGCGTCACCGGCTGGGCGGCGCACATTATCGAA
CAACGTCAGGACAACAAAATTATCCGTCCTTCCGCCAATTATGTTGGACCGGAAGACCGC
CCGTTTGTCGCGCTGGATAAGCGCCAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:389
Protein Molecular Weight:43102
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>2-methylcitrate synthase
MSDTTILQNSTHVIKPKKSVALSGVPAGNTALCTVGKSGNDLHYRGYDILDLAKHCEFEE
VAHLLIHGKLPTRDELAAYKTKLKALRGLPANVRTVLEALPAASHPMDVMRTGVSALGCT
LPEKEGHTVSGARDIADKLLASLSSILLYWYHYSHNGERIQPETDDDSIGGHFLHLLHGE
KPSQSWEKAMHISLVLYAEHEFNASTFTSRVIAGTGSDMYSAIIGAIGALRGPKHGGANE
VSLEIQQRYETPDEAEADIRKRVENKEVVIGFGHPVYTIADPRHQVIKRVAKQLSQEGGS
LKMYNIADRLETVMWESKKMFPNLDWFSAVSYNMMGVPTEMFTPLFVIARVTGWAAHIIE
QRQDNKIIRPSANYVGPEDRPFVALDKRQ
References
External Links:
ResourceLink
Uniprot ID:P31660
Uniprot Name:PRPC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674475
Ecogene ID:EG11756
Ecocyc:EG11756
ColiBase:b0333
Kegg Gene:b0333
EchoBASE ID:EB1706
CCDB:PRPC_ECOLI
BacMap:16128318
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Patton, A. J., Hough, D. W., Towner, P., Danson, M. J. (1993). "Does Escherichia coli possess a second citrate synthase gene?" Eur J Biochem 214:75-81. Pubmed: 8508809
  • Textor, S., Wendisch, V. F., De Graaf, A. A., Muller, U., Linder, M. I., Linder, D., Buckel, W. (1997). "Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria." Arch Microbiol 168:428-436. Pubmed: 9325432