o-succinylbenzoate synthase
Details
- Name
- o-succinylbenzoate synthase
- Synonyms
- 4-(2'-carboxyphenyl)-4-oxybutyric acid synthase
- 4.2.1.113
- o-succinylbenzoic acid synthase
- OSB synthase
- Gene Name
- menC
- Organism
- Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
- Amino acid sequence
>lcl|BSEQ0012239|o-succinylbenzoate synthase MAHTGRMFKIEAAEIVVARLPLKFRFETSFGVQTHKVVPLLILHGEGVQGVAEGTMEARP MYREETIAGALDLLRGTFLPAILGQTFANPEAVADALGSYRGNRMARAMVEMAAWDLWAR TLGVPLGTLLGGHKEQVEVGVSLGIQAGEQATVDLVRKHVEQGYRRIKLKIKPGWDVQPV RATREAFPDIRLTVDANSAYTLADAGRLRQLDEYDLTYIEQPLAWDDLVDHAELARRIRT PLCLDESVASAADARKALALGAGGVINLKVARVGGHAESRRVHDVAQSFGAPVWCGGMLE SGIGRAHNIHLSTLPNFRLPGDTSSASRYWERDLIQEPLEAVDGLMPVPQGPGTGVTLDR EFLATVTEAQEEHRA
- Number of residues
- 375
- Molecular Weight
- 40900.37
- Theoretical pI
- 6.3
- GO Classification
- Functionshydro-lyase activity / magnesium ion bindingProcessesmenaquinone biosynthetic process
- General Function
- Not Available
- Specific Function
- Not Available
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0012240|o-succinylbenzoate synthase (menC) ATGGCGCATACTGGCCGTATGTTCAAAATTGAAGCTGCTGAAATCGTCGTGGCGCGGCTG CCGCTCAAGTTCCGCTTTGAAACGAGTTTCGGGGTGCAAACCCACAAGGTGGTGCCGCTG CTGATTCTGCACGGTGAGGGCGTGCAGGGCGTCGCCGAGGGCACCATGGAAGCGCGGCCC ATGTACCGCGAGGAAACGATTGCCGGGGCACTGGACCTGCTGCGCGGCACCTTTTTGCCC GCCATCCTGGGGCAGACCTTCGCCAACCCCGAAGCGGTGGCGGACGCGCTCGGCAGCTAC CGGGGCAACCGCATGGCACGGGCGATGGTCGAGATGGCGGCCTGGGACCTGTGGGCGCGC ACGCTGGGGGTGCCGCTCGGGACACTGCTCGGCGGCCACAAGGAGCAGGTCGAGGTGGGG GTCAGCCTCGGCATTCAGGCGGGCGAGCAGGCGACGGTGGACCTCGTGCGAAAGCATGTC GAGCAGGGCTACCGCCGCATCAAGCTCAAGATCAAGCCCGGCTGGGACGTGCAGCCGGTA CGGGCGACCCGTGAAGCCTTTCCCGACATTCGCCTGACGGTGGACGCCAACAGCGCCTAC ACCCTGGCCGACGCCGGGCGGCTGCGGCAACTCGACGAGTACGACCTGACCTACATCGAG CAGCCGCTCGCCTGGGACGACCTCGTAGACCACGCCGAACTCGCCCGGCGCATCCGCACG CCGCTGTGCCTCGACGAGTCGGTGGCGTCGGCGGCGGACGCCCGCAAGGCGCTGGCACTG GGCGCGGGCGGCGTCATCAACCTCAAGGTGGCCCGCGTGGGCGGACACGCCGAATCGCGG CGCGTGCATGACGTGGCCCAGAGCTTCGGCGCCCCGGTGTGGTGCGGCGGGATGTTGGAG AGCGGCATCGGGCGGGCGCACAACATCCACCTCTCGACGCTGCCCAACTTCCGCTTGCCG GGCGACACCAGTTCGGCCAGCCGCTACTGGGAGCGCGACCTGATTCAGGAGCCGCTCGAA GCCGTGGACGGCCTGATGCCAGTGCCGCAGGGGCCGGGCACGGGCGTGACCCTTGACCGC GAGTTCCTGGCGACCGTCACCGAGGCGCAGGAGGAACACCGGGCGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9RYA6 UniProtKB Entry Name Q9RYA6_DEIRA GenBank Gene ID AE000513 - General References
- Wang WC, Chiu WC, Hsu SK, Wu CL, Chen CY, Liu JS, Hsu WH: Structural basis for catalytic racemization and substrate specificity of an N-acylamino acid racemase homologue from Deinococcus radiodurans. J Mol Biol. 2004 Sep 3;342(1):155-69. [Article]
- Chiu WC, You JY, Liu JS, Hsu SK, Hsu WH, Shih CH, Hwang JK, Wang WC: Structure-stability-activity relationship in covalently cross-linked N-carbamoyl D-amino acid amidohydrolase and N-acylamino acid racemase. J Mol Biol. 2006 Jun 9;359(3):741-53. Epub 2006 Apr 18. [Article]