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
- FunctionsATP binding / magnesium ion binding / manganese ion binding / pantoate-beta-alanine ligase activityProcessesbeta-alanine metabolic process / growth / pantothenate biosynthetic process / pantothenate biosynthetic process from valine / pathogenesisComponentscytosol
- 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
- Pantoate_ligase (PF02569)
- 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
Resource Link UniProtKB ID P9WIL5 UniProtKB Entry Name PANC_MYCTU - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB01930 2,4-Dihydroxy-3,3-Dimethyl-Butyrate experimental unknown Details DB02596 alpha,beta-Methyleneadenosine 5'-triphosphate experimental unknown Details DB02694 Pantoyl Adenylate experimental unknown Details DB03107 beta-Alanine experimental unknown Details