Pantothenate synthetase

NamePantothenate synthetase
Synonyms
  • 6.3.2.1
  • Pantoate--beta-alanine ligase
  • Pantoate-activating enzyme
  • PS
Gene NamepanC
OrganismMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051247|Pantothenate synthetase
MTIPAFHPGELNVYSAPGDVADVSRALRLTGRRVMLVPTMGALHEGHLALVRAAKRVPGS
VVVVSIFVNPMQFGAGEDLDAYPRTPDDDLAQLRAEGVEIAFTPTTAAMYPDGLRTTVQP
GPLAAELEGGPRPTHFAGVLTVVLKLLQIVRPDRVFFGEKDYQQLVLIRQLVADFNLDVA
VVGVPTVREADGLAMSSRNRYLDPAQRAAAVALSAALTAAAHAATAGAQAALDAARAVLD
AAPGVAVDYLELRDIGLGPMPLNGSGRLLVAARLGTTRLLDNIAIEIGTFAGTDRPDGYR
AILESHWRN
Number of residues309
Molecular Weight32677.14
Theoretical pINot Available
GO Classification
Functions
  • ATP binding
  • manganese ion binding
  • magnesium ion binding
  • pantoate-beta-alanine ligase activity
Processes
  • pantothenate biosynthetic process
  • pantothenate biosynthetic process from valine
  • beta-alanine metabolic process
  • growth
  • pathogenesis
Components
  • cytosol
General FunctionCatalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Specific FunctionAtp binding
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP9WIL5
UniProtKB Entry NamePANC_MYCTU
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0051248|Pantothenate synthetase (panC)
ATGACGATTCCTGCGTTCCATCCCGGTGAACTCAATGTGTACTCGGCACCGGGGGATGTC
GCCGATGTCAGTCGCGCACTGCGACTCACCGGCCGGCGAGTGATGTTGGTGCCTACTATG
GGTGCGCTGCACGAAGGCCACCTCGCGTTGGTGCGTGCGGCCAAGCGGGTGCCCGGATCG
GTCGTCGTCGTGTCGATCTTCGTCAACCCGATGCAATTCGGTGCCGGGGAAGATCTCGAC
GCCTATCCCCGCACCCCGGACGACGACCTGGCGCAACTGCGGGCCGAAGGCGTGGAAATC
GCTTTCACGCCAACTACCGCGGCGATGTATCCCGACGGCCTGCGCACCACCGTGCAACCC
GGTCCGTTGGCCGCCGAACTCGAGGGCGGCCCGCGGCCAACCCATTTCGCCGGCGTGCTG
ACGGTCGTGCTAAAGCTGCTGCAGATCGTGCGCCCGGATCGGGTGTTCTTCGGTGAGAAG
GACTACCAGCAGCTGGTGCTGATCCGGCAGCTGGTCGCGGACTTCAACCTCGATGTCGCG
GTGGTCGGCGTGCCGACCGTGCGCGAAGCCGACGGGCTGGCGATGTCGTCGCGCAACCGC
TACCTGGACCCGGCCCAGCGTGCGGCGGCCGTCGCGCTCTCGGCGGCGCTAACGGCCGCA
GCGCATGCGGCAACGGCTGGCGCGCAGGCCGCGCTGGATGCCGCCCGTGCGGTGCTCGAC
GCTGCACCCGGCGTGGCGGTCGACTACCTGGAGCTGCGCGATATCGGGCTTGGCCCGATG
CCGCTCAACGGTTCCGGTCGGCTGCTGGTTGCTGCCCGGCTTGGCACCACCAGGCTGCTG
GACAACATTGCGATTGAAATCGGAACTTTCGCCGGCACCGACCGCCCGGACGGATACCGG
GCAATCCTCGAATCACATTGGAGAAACTGA
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. 9634230
  2. Zheng R, Blanchard JS: Steady-state and pre-steady-state kinetic analysis of Mycobacterium tuberculosis pantothenate synthetase. Biochemistry. 2001 Oct 30;40(43):12904-12. 11669627
  3. Sambandamurthy VK, Wang X, Chen B, Russell RG, Derrick S, Collins FM, Morris SL, Jacobs WR Jr: A pantothenate auxotroph of Mycobacterium tuberculosis is highly attenuated and protects mice against tuberculosis. Nat Med. 2002 Oct;8(10):1171-4. Epub 2002 Sep 9. 12219086
  4. Zheng R, Dam TK, Brewer CF, Blanchard JS: Active site residues in Mycobacterium tuberculosis pantothenate synthetase required in the formation and stabilization of the adenylate intermediate. Biochemistry. 2004 Jun 8;43(22):7171-8. 15170354
  5. Raman K, Yeturu K, Chandra N: targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis. BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109. 19099550
  6. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. 21969609
  7. Dillon NA, Peterson ND, Rosen BC, Baughn AD: Pantothenate and pantetheine antagonize the antitubercular activity of pyrazinamide. Antimicrob Agents Chemother. 2014 Dec;58(12):7258-63. doi: 10.1128/AAC.04028-14. Epub 2014 Sep 22. 25246400
  8. Wang S, Eisenberg D: Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate. Protein Sci. 2003 May;12(5):1097-108. 12717031
  9. Wang S, Eisenberg D: Crystal structure of the pantothenate synthetase from Mycobacterium tuberculosis, snapshots of the enzyme in action. Biochemistry. 2006 Feb 14;45(6):1554-61. 16460002