Pantothenate synthetase

Details

Name
Pantothenate synthetase
Synonyms
  • 6.3.2.1
  • Pantoate--beta-alanine ligase
  • Pantoate-activating enzyme
  • PS
Gene Name
panC
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051247|Pantothenate synthetase
MTIPAFHPGELNVYSAPGDVADVSRALRLTGRRVMLVPTMGALHEGHLALVRAAKRVPGS
VVVVSIFVNPMQFGAGEDLDAYPRTPDDDLAQLRAEGVEIAFTPTTAAMYPDGLRTTVQP
GPLAAELEGGPRPTHFAGVLTVVLKLLQIVRPDRVFFGEKDYQQLVLIRQLVADFNLDVA
VVGVPTVREADGLAMSSRNRYLDPAQRAAAVALSAALTAAAHAATAGAQAALDAARAVLD
AAPGVAVDYLELRDIGLGPMPLNGSGRLLVAARLGTTRLLDNIAIEIGTFAGTDRPDGYR
AILESHWRN
Number of residues
309
Molecular Weight
32677.14
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / magnesium ion binding / manganese ion binding / pantoate-beta-alanine ligase activity
Processes
beta-alanine metabolic process / growth / pantothenate biosynthetic process / pantothenate biosynthetic process from valine / pathogenesis
Components
cytosol
General Function
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Specific Function
Atp binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0051248|Pantothenate synthetase (panC)
ATGACGATTCCTGCGTTCCATCCCGGTGAACTCAATGTGTACTCGGCACCGGGGGATGTC
GCCGATGTCAGTCGCGCACTGCGACTCACCGGCCGGCGAGTGATGTTGGTGCCTACTATG
GGTGCGCTGCACGAAGGCCACCTCGCGTTGGTGCGTGCGGCCAAGCGGGTGCCCGGATCG
GTCGTCGTCGTGTCGATCTTCGTCAACCCGATGCAATTCGGTGCCGGGGAAGATCTCGAC
GCCTATCCCCGCACCCCGGACGACGACCTGGCGCAACTGCGGGCCGAAGGCGTGGAAATC
GCTTTCACGCCAACTACCGCGGCGATGTATCCCGACGGCCTGCGCACCACCGTGCAACCC
GGTCCGTTGGCCGCCGAACTCGAGGGCGGCCCGCGGCCAACCCATTTCGCCGGCGTGCTG
ACGGTCGTGCTAAAGCTGCTGCAGATCGTGCGCCCGGATCGGGTGTTCTTCGGTGAGAAG
GACTACCAGCAGCTGGTGCTGATCCGGCAGCTGGTCGCGGACTTCAACCTCGATGTCGCG
GTGGTCGGCGTGCCGACCGTGCGCGAAGCCGACGGGCTGGCGATGTCGTCGCGCAACCGC
TACCTGGACCCGGCCCAGCGTGCGGCGGCCGTCGCGCTCTCGGCGGCGCTAACGGCCGCA
GCGCATGCGGCAACGGCTGGCGCGCAGGCCGCGCTGGATGCCGCCCGTGCGGTGCTCGAC
GCTGCACCCGGCGTGGCGGTCGACTACCTGGAGCTGCGCGATATCGGGCTTGGCCCGATG
CCGCTCAACGGTTCCGGTCGGCTGCTGGTTGCTGCCCGGCTTGGCACCACCAGGCTGCTG
GACAACATTGCGATTGAAATCGGAACTTTCGCCGGCACCGACCGCCCGGACGGATACCGG
GCAATCCTCGAATCACATTGGAGAAACTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WIL5
UniProtKB Entry NamePANC_MYCTU
General 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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB019302,4-Dihydroxy-3,3-Dimethyl-ButyrateexperimentalunknownDetails
DB02596alpha,beta-Methyleneadenosine 5'-triphosphateexperimentalunknownDetails
DB02694Pantoyl AdenylateexperimentalunknownDetails
DB03107beta-AlanineexperimentalunknownDetails