2-methylcitrate synthase
Details
- Name
- 2-methylcitrate synthase
- Synonyms
- (2S,3S)-2-methylcitrate synthase
- 2-MCS
- 2.3.3.5
- cisY
- Citrate synthase
- Gene Name
- gltA
- Organism
- Antarctic bacterium DS2-3R
- Amino acid sequence
>lcl|BSEQ0016866|2-methylcitrate synthase MTEPTIHKGLAGVTADVTAISKVNSDTNSLLYRGYPVQELAAKCSFEQVAYLLWNSELPN DSELKAFVNFERSHRKLDENVKGAIDLLSTACHPMDVARTAVSVLGANHARAQDSSPEAN LEKAMSLLATFPSVVAYDQRRRRGEELIEPREDLDYSANFLWMTFGEEAAPEVVEAFNVS MILYAEHSFNASTFTARVITSTLADLHSAVTGAIGALKGPLHGGANEAVMHTFEEIGIRK DESLDEAATRSKAWMVDALAQKKKVMGFGHRVYKNGDSRVPTMKSALDAMIKHYDRPEML GLYNGLEAAMEEAKQIKPNLDYPAGPTYNLMGFDTEMFTPLFIAARITGWTAHIMEQVAD NALIRPLSEYNGPEQRQVP
- Number of residues
- 379
- Molecular Weight
- 41832.0
- Theoretical pI
- 5.17
- GO Classification
- Functions2-methylcitrate synthase activity / citrate synthase activityProcessespropionate metabolic process, methylcitrate cycle / tricarboxylic acid cycleComponentscytoplasm
- General Function
- Citrate synthase activity
- Specific Function
- Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield (2S,3S)-2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity.
- Pfam Domain Function
- Citrate_synt (PF00285)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0005275|1140 bp ATGACCGAACCAACAATTCATAAGGGCCTTGCCGGCGTCACGGCGGATGTCACCGCCATT TCGAAGGTCAATTCTGATACCAACTCGCTGCTGTACCGTGGATACCCCGTTCAGGAACTG GCTGCTAAGTGCAGCTTTGAACAGGTGGCCTACTTGCTGTGGAACAGCGAACTGCCCAAC GATTCCGAGCTGAAAGCTTTCGTAAATTTCGAACGCTCCCACCGGAAACTGGATGAGAAC GTCAAAGGGGCAATAGACCTCCTCTCCACTGCCTGTCACCCTATGGACGTTGCGCGGACC GCCGTCTCAGTTCTGGGAGCCAACCACGCCAGGGCGCAGGATTCCTCCCCGGAAGCAAAT CTAGAAAAGGCGATGTCGCTGCTGGCAACCTTCCCGTCCGTCGTCGCCTACGACCAAAGG CGACGACGCGGTGAGGAACTTATCGAACCACGAGAGGATCTCGATTACTCCGCGAACTTC CTGTGGATGACTTTTGGCGAAGAGGCAGCGCCGGAGGTTGTGGAAGCCTTCAACGTCTCC ATGATTCTCTACGCGGAGCATTCCTTCAACGCCTCGACGTTCACGGCCCGGGTCATCACC TCCACCCTGGCGGATCTGCATTCGGCGGTGACCGGAGCCATAGGTGCCCTCAAGGGGCCG CTGCACGGGGGTGCCAACGAGGCCGTGATGCATACCTTTGAGGAGATTGGGATCCGCAAG GACGAATCCCTCGATGAGGCAGCCACGCGTTCGAAAGCTTGGATGGTCGATGCCCTTGCG CAGAAGAAAAAGGTCATGGGTTTTGGGCACCGCGTGTACAAGAATGGTGACTCCCGGGTC CCCACCATGAAGAGCGCTCTGGACGCCATGATCAAACATTATGATCGTCCGGAAATGCTC GGCCTGTACAACGGACTCGAAGCCGCTATGGAAGAGGCCAAGCAGATCAAGCCGAATCTC GACTACCCGGCAGGACCCACCTATAACCTGATGGGCTTTGACACGGAGATGTTCACTCCG CTCTTCATCGCCGCGCGCATCACCGGTTGGACCGCCCATATCATGGAACAAGTGGCGGAC AACGCTCTGATCCGCCCACTCAGCGAATATAACGGTCCTGAGCAGCGCCAGGTCCCCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID O34002 UniProtKB Entry Name PRPC_ABDS2 GenBank Gene ID U85944 - General References
- Gerike U, Danson MJ, Russell NJ, Hough DW: Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R. Eur J Biochem. 1997 Aug 15;248(1):49-57. [Article]
- Gerike U, Hough DW, Russell NJ, Dyall-Smith ML, Danson MJ: Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships. Microbiology. 1998 Apr;144 ( Pt 4):929-35. [Article]
- Russell RJ, Gerike U, Danson MJ, Hough DW, Taylor GL: Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure. 1998 Mar 15;6(3):351-61. [Article]