Coenzyme A biosynthesis bifunctional protein CoaBC
Details
- Name
- Coenzyme A biosynthesis bifunctional protein CoaBC
- Synonyms
- dfp
- DNA/pantothenate metabolism flavoprotein
- Gene Name
- coaBC
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0003996|Coenzyme A biosynthesis bifunctional protein CoaBC MSLAGKKIVLGVSGGIAAYKTPELVRRLRDRGADVRVAMTEAAKAFITPLSLQAVSGYPV SDSLLDPAAEAAMGHIELGKWADLVILAPATADLIARVAAGMANDLVSTICLATPAPVAV LPAMNQQMYRAAATQHNLEVLASRGLLIWGPDSGSQACGDIGPGRMLDPLTIVDMAVAHF SPVNDLKHLNIMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAARRGANVTLVSGPVSL PTPPFVKRVDVMTALEMEAAVNASVQQQNIFIGCAAVADYRAATVAPEKIKKQATQGDEL TIKMVKNPDIVAGVAALKDHRPYVVGFAAETNNVEEYARQKRIRKNLDLICANDVSQPTQ GFNSDNNALHLFWQDGDKVLPLERKELLGQLLLDEIVTRYDEKNRR
- Number of residues
- 406
- Molecular Weight
- 43437.685
- Theoretical pI
- 7.58
- GO Classification
- FunctionsFMN binding / metal ion binding / phosphopantothenate--cysteine ligase activity / phosphopantothenoylcysteine decarboxylase activityProcessescoenzyme A biosynthetic process / pantothenate catabolic processComponentscytosol
- General Function
- Phosphopantothenoylcysteine decarboxylase activity
- Specific Function
- Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011457|Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC) ATGAGCCTGGCCGGTAAAAAAATCGTTCTCGGCGTTAGCGGCGGTATTGCTGCCTATAAA ACCCCTGAACTGGTGCGTCGTTTGCGCGATCGCGGGGCCGACGTCCGCGTAGCCATGACC GAAGCGGCAAAAGCCTTTATCACCCCACTTAGCTTGCAGGCGGTTTCTGGTTATCCCGTT TCCGACAGTCTGCTGGACCCGGCAGCCGAAGCCGCTATGGGCCATATTGAGCTGGGTAAA TGGGCTGATTTAGTGATTCTCGCCCCTGCCACGGCAGATTTGATTGCCCGTGTTGCTGCC GGAATGGCGAATGACCTGGTATCGACGATTTGTCTGGCTACACCTGCGCCTGTAGCCGTG CTCCCCGCCATGAACCAGCAGATGTACCGTGCCGCTGCCACGCAGCATAATTTAGAGGTG CTTGCTTCCCGTGGTTTGCTCATCTGGGGGCCAGACAGTGGCAGTCAGGCTTGTGGTGAT ATCGGTCCTGGGCGAATGCTCGATCCGTTAACCATTGTGGATATGGCGGTAGCGCATTTT TCGCCCGTCAACGACCTGAAACATCTGAACATTATGATTACCGCCGGCCCGACGCGTGAA CCGCTCGATCCGGTGCGTTATATCTCTAATCACAGCTCCGGCAAGATGGGTTTTGCTATC GCCGCCGCCGCTGCCCGTCGTGGCGCGAACGTCACGCTGGTATCAGGTCCGGTTTCACTA CCGACGCCACCGTTTGTTAAACGTGTTGATGTGATGACCGCGCTGGAAATGGAAGCCGCC GTGAATGCTTCTGTACAGCAGCAAAATATTTTTATCGGCTGCGCCGCCGTGGCGGATTAT CGCGCAGCTACCGTGGCCCCAGAGAAAATCAAAAAGCAGGCCACGCAGGGTGATGAATTA ACAATAAAAATGGTTAAAAACCCCGATATCGTCGCAGGCGTTGCCGCACTAAAAGACCAT CGACCCTACGTCGTTGGATTTGCCGCCGAAACAAATAATGTGGAAGAATACGCCCGGCAA AAACGTATCCGTAAAAACCTTGATCTGATCTGCGCGAACGATGTTTCCCAGCCAACTCAA GGATTTAACAGCGACAACAACGCATTACACCTTTTCTGGCAGGACGGAGATAAAGTCTTA CCGCTTGAGCGCAAAGAGCTCCTTGGCCAATTATTACTCGACGAGATCGTGACCCGTTAT GATGAAAAAAATCGACGTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0ABQ0 UniProtKB Entry Name COABC_ECOLI GenBank Gene ID L10328 - General References
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- Kupke T: Active-site residues and amino acid specificity of the bacterial 4'-phosphopantothenoylcysteine synthetase CoaB. Eur J Biochem. 2004 Jan;271(1):163-72. [Article]
- Stanitzek S, Augustin MA, Huber R, Kupke T, Steinbacher S: Structural basis of CTP-dependent peptide bond formation in coenzyme A biosynthesis catalyzed by Escherichia coli PPC synthetase. Structure. 2004 Nov;12(11):1977-88. [Article]