Citrate synthase

Name	Citrate 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	None
Molecular Weight	41832.0
Theoretical pI	5.17
GO Classification	Functions 2-methylcitrate synthase activity citrate synthase activity Processes tricarboxylic acid cycle propionate metabolic process, methylcitrate cycle Components cytoplasm
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.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	O34002
UniProtKB Entry Name
Cellular Location	None
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
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
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. [9310359 ] 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. [9579066 ] 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. [9551556 ]

From www.t3db.ca