Coenzyme A biosynthesis bifunctional protein coaBC (P0ABQ0)

Identification
Name:Coenzyme A biosynthesis bifunctional protein coaBC
Synonyms:
  • DNA/pantothenate metabolism flavoprotein
  • Phosphopantothenoylcysteine decarboxylase
  • PPCDC
  • CoaC
  • Phosphopantothenate--cysteine ligase
  • CoaB
  • PPC synthetase
  • PPCS
  • Phosphopantothenoylcysteine synthase
Gene Name:coaBC
Enzyme Class:
Biological Properties
General Function:Involved in phosphopantothenate--cysteine ligase 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
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0D-4'-Phosphopantothenate + 1.0Cytidine triphosphate + 1.0L-Cysteine → 1.04-Phosphopantothenoylcysteine + 1.0Cytidine monophosphate + 1.0Hydrogen ion + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.04-Phosphopantothenoylcysteine + 1.0Hydrogen ion ↔ 1.0Carbon dioxide + 1.0Pantetheine 4'-phosphate + 1.0pantotheine 4'-phosphate
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.04-Phosphopantothenoylcysteine ↔ 1.0Pantetheine 4'-phosphate + 1.0Carbon dioxide
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0D-4'-Phosphopantothenate + 1.0L-Cysteine ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.04-Phosphopantothenoylcysteine
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Cytidine triphosphate + 1.0D-4'-Phosphopantothenate + 1.0L-Cysteine ↔ 1.0Cytidine monophosphate + 1.0Pyrophosphate + 1.04-Phosphopantothenoylcysteine
ReactionCard
SMPDB Reactions:
1.0Thumb → 1.0Pantetheine 4'-phosphate+1.0Thumb+1.0Thumb
1.04-Phosphopantothenoylcysteine → 1.0Pantetheine 4'-phosphate + 1.0Carbon dioxide + 1.0pantotheine 4'-phosphate
ReactionCard
1.0D-4'-Phosphopantothenate+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Cytidine monophosphate+1.0Pyrophosphate+1.0Thumb+1.0Thumb+1.0Thumb
1.0D-4'-Phosphopantothenate + 1.0Cytidine triphosphate + 1.0L-Cysteine + 1.0D-4'-Phosphopantothenate → 1.0Cytidine monophosphate + 1.0Pyrophosphate + 1.0Hydrogen ion + 1.04-Phosphopantothenoylcysteine + 1.0Cytidine monophosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.04'-phosphopantetheine+1.0Thumb
1.04-Phosphopantothenoylcysteine + 1.0Hydrogen ion → 1.0Carbon dioxide + 1.04'-phosphopantetheine + 1.04'-phosphopantetheine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0D-4'-Phosphopantothenate + 1.0Cytidine triphosphate + 1.0L-Cysteine → 1.04-Phosphopantothenoylcysteine + 1.0Cytidine monophosphate + 1.0Hydrogen ion + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.04-Phosphopantothenoylcysteine + 1.0Hydrogen ion ↔ 1.0Carbon dioxide + 1.0Pantetheine 4'-phosphate + 1.0pantotheine 4'-phosphate
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.04-Phosphopantothenoylcysteine → 1.0pantotheine 4'-phosphate + 1.0Carbon dioxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB242134'-phosphopantetheineMetaboCard
ECMDB011174-PhosphopantothenoylcysteineMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB00095Cytidine monophosphateMetaboCard
ECMDB00082Cytidine triphosphateMetaboCard
ECMDB01016D-4'-PhosphopantothenateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00574L-CysteineMetaboCard
ECMDB01416Pantetheine 4'-phosphateMetaboCard
ECMDB23216pantotheine 4'-phosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Function
acid-amino acid ligase activity
binding
carbon-carbon lyase activity
carboxy-lyase activity
catalytic activity
FMN binding
ligase activity
ligase activity, forming carbon-nitrogen bonds
lyase activity
nucleotide binding
phosphopantothenate--cysteine ligase activity
phosphopantothenoylcysteine decarboxylase activity
Process
cellular metabolic process
coenzyme A biosynthetic process
coenzyme biosynthetic process
coenzyme catabolic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
pantothenate catabolic process
Gene Properties
Blattner:b3639
Gene OrientationClockwise
Centisome Percentage:82.13
Left Sequence End3810754
Right Sequence End3811974
Gene Sequence:
>1221 bp
ATGTTTAAGTCTTTTTTCCCAAAGCCGGGAACGTTTTTTCTCTCGGCCTTCGTTTGGGCA
TTGATTGCCGTTATCTTCTGGCAAGCCGGTGGGGGTGACTGGGTGGCGCGTATCACCGGC
GCTTCCGGGCAGATCCCGATTAGCGCCGCGCGTTTCTGGTCGTTGGATTTCCTGATTTTT
TACGCTTACTACATTGTTTGCGTAGGACTTTTTGCATTGTTCTGGTTTATCTACAGCCCG
CATCGTTGGCAATACTGGTCAATACTCGGTACTGCACTGATCATCTTCGTCACCTGGTTT
TTGGTGGAAGTCGGGGTCGCCGTCAACGCCTGGTATGCGCCGTTCTATGATCTGATTCAA
ACCGCGCTAAGTTCGCCGCATAAAGTCACCATCGAACAATTTTACCGCGAAGTGGGCGTC
TTTCTGGGGATTGCGCTGATCGCTGTGGTGATCAGTGTGCTGAACAACTTCTTTGTCAGT
CACTACGTGTTCCGCTGGCGTACAGCGATGAACGAATATTACATGGCGAACTGGCAACAA
CTGCGTCATATCGAAGGGGCCGCACAGCGTGTGCAGGAAGACACCATGCGTTTTGCTTCA
ACGCTGGAGAATATGGGCGTCAGTTTTATCAACGCCATCATGACGTTGATCGCCTTCCTG
CCGGTGCTGGTAACGCTCTCCGCGCATGTGCCGGAGCTGCCGATTATCGGGCACATTCCG
TATGGTCTGGTGATTGCCGCAATCGTCTGGTCGCTGATGGGGACCGGATTGCTGGCAGTG
GTAGGGATCAAACTGCCGGGGCTGGAGTTTAAAAACCAGCGTGTAGAGGCTGCCTACCGT
AAAGAGCTGGTTTATGGTGAAGACGATGCCACGCGCGCGACGCCGCCTACGGTACGCGAG
CTGTTTAGCGCCGTACGGAAAAACTATTTCCGCCTCTATTTTCACTATATGTATTTCAAC
ATCGCCCGCATTCTCTATTTGCAGGTCGATAACGTTTTCGGTTTGTTCTTGCTGTTTCCG
TCAATTGTTGCCGGTACGATTACGCTCGGCCTGATGACGCAGATTACCAACGTTTTTGGT
CAGGTTCGCGGTGCTTTCCAGTACCTGATTAACTCATGGACCACACTGGTTGAGTTGATG
TCTATCTACAAACGTCTGCGCAGCTTTGAACATGAGCTGGATGGTGACAAAATTCAGGAA
GTAACCCATACCTTGAGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:406
Protein Molecular Weight:43438
Protein Theoretical pI:8
PDB File:1U80
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Coenzyme A biosynthesis bifunctional protein coaBC
MSLAGKKIVLGVSGGIAAYKTPELVRRLRDRGADVRVAMTEAAKAFITPLSLQAVSGYPV
SDSLLDPAAEAAMGHIELGKWADLVILAPATADLIARVAAGMANDLVSTICLATPAPVAV
LPAMNQQMYRAAATQHNLEVLASRGLLIWGPDSGSQACGDIGPGRMLDPLTIVDMAVAHF
SPVNDLKHLNIMITAGPTREPLDPVRYISNHSSGKMGFAIAAAAARRGANVTLVSGPVSL
PTPPFVKRVDVMTALEMEAAVNASVQQQNIFIGCAAVADYRAATVAPEKIKKQATQGDEL
TIKMVKNPDIVAGVAALKDHRPYVVGFAAETNNVEEYARQKRIRKNLDLICANDVSQPTQ
GFNSDNNALHLFWQDGDKVLPLERKELLGQLLLDEIVTRYDEKNRR
References
External Links:
ResourceLink
Uniprot ID:P0ABQ0
Uniprot Name:COABC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674518
PDB ID:1U80
Ecogene ID:EG10004
Ecocyc:EG10004
ColiBase:b3639
Kegg Gene:b3639
EchoBASE ID:EB0004
CCDB:COABC_ECOLI
BacMap:90111624
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kupke, T. (2001). "Molecular characterization of the 4'-phosphopantothenoylcysteine decarboxylase domain of bacterial Dfp flavoproteins." J Biol Chem 276:27597-27604. Pubmed: 11358972
  • Kupke, T. (2002). "Molecular characterization of the 4'-phosphopantothenoylcysteine synthetase domain of bacterial dfp flavoproteins." J Biol Chem 277:36137-36145. Pubmed: 12140293
  • Kupke, T. (2004). "Active-site residues and amino acid specificity of the bacterial 4'-phosphopantothenoylcysteine synthetase CoaB." Eur J Biochem 271:163-172. Pubmed: 14686929
  • Kupke, T., Uebele, M., Schmid, D., Jung, G., Blaesse, M., Steinbacher, S. (2000). "Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals a function for bacterial Dfp proteins in coenzyme A biosynthesis." J Biol Chem 275:31838-31846. Pubmed: 10922366
  • Lundberg, L. G., Thoresson, H. O., Karlstrom, O. H., Nyman, P. O. (1983). "Nucleotide sequence of the structural gene for dUTPase of Escherichia coli K-12." EMBO J 2:967-971. Pubmed: 6139280
  • Stanitzek, S., Augustin, M. A., Huber, R., Kupke, T., Steinbacher, S. (2004). "Structural basis of CTP-dependent peptide bond formation in coenzyme A biosynthesis catalyzed by Escherichia coli PPC synthetase." Structure 12:1977-1988. Pubmed: 15530362
  • Strauss, E., Kinsland, C., Ge, Y., McLafferty, F. W., Begley, T. P. (2001). "Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria." J Biol Chem 276:13513-13516. Pubmed: 11278255