Pentaerythritol tetranitrate reductase

Details

Name
Pentaerythritol tetranitrate reductase
Kind
protein
Synonyms
Not Available
Gene Name
onr
UniProtKB Entry
P71278TrEMBL
Organism
Enterobacter cloacae
NCBI Taxonomy ID
550
Amino acid sequence
>lcl|BSEQ0021993|Pentaerythritol tetranitrate reductase
MSAEKLFTPLKVGAVTAPNRVFMAPLTRLRSIEPGDIPTPLMGEYYRQRASAGLIISEAT
QISAQAKGYAGAPGLHSPEQIAAWKKITAGVHAEDGRIAVQLWHTGRISHSSIQPGGQAP
VSASALNANTRTSLRDENGNAIRVDTTTPRALELDEIPGIVNDFRQAVANAREAGFDLVE
LHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAVCNEWSADRIGIRVSPIGT
FQNVDNGPNEEADALYLIEELAKRGIAYLHMSETDLAGGKPYSEAFRQKVRERFHGVIIG
AGAYTAEKAEDLIGKGLIDAVAFGRDYIANPDLVARLQKKAELNPQRPESFYGGGAEGYT
DYPSL
Number of residues
365
Molecular Weight
39488.93
Theoretical pI
6.06
GO Classification
Functions
FMN binding / oxidoreductase activity
General Function
Not Available
Specific Function
FMN binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0004906|1098 bp
ATGTCCGCTGAAAAGCTGTTTACCCCACTGAAAGTGGGTGCCGTTACTGCCCCAAACCGC
GTGTTTATGGCCCCACTTACCCGTCTGCGCAGCATCGAGCCGGGCGATATCCCAACGCCA
TTGATGGGTGAGTATTACCGCCAGCGCGCCAGCGCGGGCCTGATTATCTCCGAAGCCACG
CAGATTTCTGCTCAGGCAAAAGGCTACGCCGGTGCACCGGGTCTGCACAGCCCGGAACAG
ATCGCCGCGTGGAAAAAAATCACCGCAGGCGTGCATGCTGAAGATGGCCGTATTGCGGTT
CAGCTGTGGCACACCGGTCGTATCTCACACAGCAGCATCCAGCCTGGCGGTCAGGCGCCG
GTTTCTGCCTCTGCCCTGAACGCCAATACCCGCACTTCCCTGCGCGATGAAAACGGTAAT
GCGATCCGCGTCGACACCACCACGCCACGCGCGCTGGAGCTGGACGAGATCCCGGGTATC
GTGAATGATTTCCGTCAGGCCGTCGCCAACGCCCGGGAAGCGGGCTTCGACCTGGTTGAG
CTTCACTCTGCGCACGGTTACCTGCTGCATCAGTTCCTGTCCCCGTCTTCCAACCAGCGT
ACCGACCAGTACGGCGGCAGCGTTGAAAACCGCGCGCGTCTGGTGCTTGAAGTGGTGGAT
GCTGTCTGTAATGAGTGGAGCGCAGACCGCATTGGTATTCGTGTCTCCCCGATCGGTACT
TTCCAGAACGTCGACAACGGTCCGAACGAAGAAGCAGACGCGCTGTATCTGATTGAAGAG
CTGGCGAAACGCGGTATCGCCTATCTGCACATGTCCGAGACGGACTTGGCAGGCGGCAAG
CCTTACAGTGAAGCCTTCCGTCAGAAAGTGCGCGAGCGCTTCCACGGCGTGATTATCGGG
GCGGGTGCGTATACGGCAGAAAAAGCCGAGGATTTGATCGGTAAAGGCCTGATCGACGCC
GTGGCCTTTGGCCGTGACTACATTGCTAACCCGGATCTGGTTGCCCGTTTGCAGAAAAAA
GCCGAACTGAACCCGCAGCGTCCTGAAAGCTTCTATGGCGGCGGCGCGGAAGGTTATACC
GACTACCCTTCACTGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP71278
UniProtKB Entry NameP71278_ENTCL
GenBank Gene IDU68759
PDB ID(s)1GVO, 1GVQ, 1GVR, 1GVS, 1H50, 1H51, 1H60, 1H61, 1H62, 1H63, 1VYP, 1VYR, 1VYS, 2ABA, 2ABB, 3F03, 3KFT, 3P62, 3P67, 3P74, 3P7Y, 3P80, 3P81, 3P82, 3P84, 3P8I, 3P8J
General References
  1. Barna TM, Khan H, Bruce NC, Barsukov I, Scrutton NS, Moody PC: Crystal structure of pentaerythritol tetranitrate reductase: "flipped" binding geometries for steroid substrates in different redox states of the enzyme. J Mol Biol. 2001 Jul 6;310(2):433-47. [Article]
  2. Khan H, Harris RJ, Barna T, Craig DH, Bruce NC, Munro AW, Moody PC, Scrutton NS: Kinetic and structural basis of reactivity of pentaerythritol tetranitrate reductase with NADPH, 2-cyclohexenone, nitroesters, and nitroaromatic explosives. J Biol Chem. 2002 Jun 14;277(24):21906-12. Epub 2002 Mar 28. [Article]
  3. Khan H, Barna T, Harris RJ, Bruce NC, Barsukov I, Munro AW, Moody PC, Scrutton NS: Atomic resolution structures and solution behavior of enzyme-substrate complexes of Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase. Multiple conformational states and implications for the mechanism of nitroaromatic explosive degradation. J Biol Chem. 2004 Jul 16;279(29):30563-72. Epub 2004 May 5. [Article]
  4. Khan H, Barna T, Bruce NC, Munro AW, Leys D, Scrutton NS: Proton transfer in the oxidative half-reaction of pentaerythritol tetranitrate reductase. Structure of the reduced enzyme-progesterone complex and the roles of residues Tyr186, His181, His184. FEBS J. 2005 Sep;272(18):4660-71. [Article]
  5. Pudney CR, Hay S, Levy C, Pang J, Sutcliffe MJ, Leys D, Scrutton NS: Evidence to support the hypothesis that promoting vibrations enhance the rate of an enzyme catalyzed H-tunneling reaction. J Am Chem Soc. 2009 Dec 2;131(47):17072-3. doi: 10.1021/ja908469m. [Article]
  6. Hulley ME, Toogood HS, Fryszkowska A, Mansell D, Stephens GM, Gardiner JM, Scrutton NS: Focused directed evolution of pentaerythritol tetranitrate reductase by using automated anaerobic kinetic screening of site-saturated libraries. Chembiochem. 2010 Nov 22;11(17):2433-47. doi: 10.1002/cbic.201000527. [Article]
  7. Toogood HS, Fryszkowska A, Hulley M, Sakuma M, Mansell D, Stephens GM, Gardiner JM, Scrutton NS: A site-saturated mutagenesis study of pentaerythritol tetranitrate reductase reveals that residues 181 and 184 influence ligand binding, stereochemistry and reactivity. Chembiochem. 2011 Mar 21;12(5):738-49. doi: 10.1002/cbic.201000662. Epub 2011 Mar 4. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
TrinitrotolueneexperimentalunknowntargetDetails
CyclohexanoneexperimentalunknowntargetDetails
Flavin mononucleotideapproved, investigationalunknowntargetDetails
Picric acidexperimentalunknowntargetDetails
2,4-DinitrophenolexperimentalunknowntargetDetails
BoldioneexperimentalunknowntargetDetails
Isopentyl PyrophosphateexperimentalunknowntargetDetails
Potassium nitrateapprovedunknownenzymesubstrateDetails