2-methylisocitrate lyase
Details
- Name
- 2-methylisocitrate lyase
- Synonyms
- (2R,3S)-2-methylisocitrate lyase
- 2-MIC
- 4.1.3.30
- yahQ
- Gene Name
- prpB
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0010879|2-methylisocitrate lyase MSLHSPGKAFRAALTKENPLQIVGTINANHALLAQRAGYQAIYLSGGGVAAGSLGLPDLG ISTLDDVLTDIRRITDVCSLPLLVDADIGFGSSAFNVARTVKSMIKAGAAGLHIEDQVGA KRCGHRPNKAIVSKEEMVDRIRAAVDAKTDPDFVIMARTDALAVEGLDAAIERAQAYVEA GAEMLFPEAITELAMYRQFADAVQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAF RAMNRAAEHVYNVLRQEGTQKSVIDTMQTRNELYESINYYQYEEKLDNLFARSQVK
- Number of residues
- 296
- Molecular Weight
- 32134.305
- Theoretical pI
- 5.4
- GO Classification
- Functionsmagnesium ion binding / methylisocitrate lyase activity / transferase activity, transferring acyl groups, acyl groups converted into alkyl on transferProcessesglyoxylate cycle / propionate catabolic process, 2-methylcitrate cycleComponentscytoplasm
- General Function
- Transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
- Specific Function
- Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-carbanion intermediate.
- Pfam Domain Function
- ICL (PF00463)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0010880|2-methylisocitrate lyase (prpB) ATGTCTCTACACTCTCCAGGTAAAGCGTTTCGCGCTGCACTGACTAAAGAAAATCCATTG CAGATTGTTGGCACCATCAACGCTAATCATGCGCTGTTGGCGCAGCGTGCCGGATATCAG GCAATTTATCTTTCTGGCGGTGGCGTGGCGGCAGGTTCGCTGGGGCTGCCCGATCTCGGT ATTTCTACCCTTGATGATGTGCTGACCGACATTCGCCGTATCACCGACGTTTGTTCGCTG CCGCTGCTGGTGGATGCGGATATCGGTTTTGGTTCTTCGGCCTTTAACGTGGCGCGCACC GTGAAATCGATGATTAAAGCCGGTGCGGCAGGATTGCATATTGAAGATCAGGTTGGTGCG AAACGCTGCGGTCATCGTCCGAATAAAGCGATCGTCTCGAAAGAAGAGATGGTGGATCGG ATCCGCGCGGCGGTGGATGCGAAAACCGATCCTGATTTTGTGATCATGGCGCGCACCGAT GCTCTGGCGGTAGAGGGGCTGGATGCGGCGATCGAGCGTGCGCAGGCCTATGTTGAAGCG GGTGCCGAGATGTTGTTCCCGGAGGCGATTACCGAACTCGCCATGTACCGCCAGTTTGCC GATGCGGTGCAGGTGCCGATCCTCGCCAACATCACCGAATTTGGTGCCACGCCGCTGTTT ACCACCGACGAATTACGCAGCGCCCATGTCGCAATGGCGCTGTACCCACTTTCAGCGTTC CGCGCCATGAACCGCGCCGCTGAACATGTCTACAACGTCCTGCGCCAGGAAGGCACGCAG AAAAGCGTCATCGACACCATGCAGACCCGCAACGAGCTGTACGAAAGCATCAACTACTAC CAGTACGAAGAGAAGCTCGACAACCTGTTTGCCCGTAGCCAGGTGAAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P77541 UniProtKB Entry Name PRPB_ECOLI GenBank Protein ID 1657527 GenBank Gene ID U73857 - General References
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Textor S, Wendisch VF, De Graaf AA, Muller U, Linder MI, Linder D, Buckel W: Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. Arch Microbiol. 1997 Nov;168(5):428-36. [Article]
- Brock M, Darley D, Textor S, Buckel W: 2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: characterization and comparison of both enzymes. Eur J Biochem. 2001 Jun;268(12):3577-86. [Article]
- Grimm C, Evers A, Brock M, Maerker C, Klebe G, Buckel W, Reuter K: Crystal structure of 2-methylisocitrate lyase (PrpB) from Escherichia coli and modelling of its ligand bound active centre. J Mol Biol. 2003 May 2;328(3):609-21. [Article]
- Liu S, Lu Z, Han Y, Melamud E, Dunaway-Mariano D, Herzberg O: Crystal structures of 2-methylisocitrate lyase in complex with product and with isocitrate inhibitor provide insight into lyase substrate specificity, catalysis and evolution. Biochemistry. 2005 Mar 1;44(8):2949-62. [Article]