1-deoxypentalenic acid 11-beta-hydroxylase
Details
- Name
- 1-deoxypentalenic acid 11-beta-hydroxylase
- Kind
- protein
- Synonyms
- 1.14.11.35
- Neopentalenolactone biosynthesis protein H
- Gene Name
- ptlH
- UniProtKB Entry
- Q82IZ1Swiss-Prot
- Organism
- Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
- NCBI Taxonomy ID
- 227882
- Amino acid sequence
>lcl|BSEQ0012617|1-deoxypentalenic acid 11-beta-hydroxylase MTNVTGDYTDCTPLLGDRAALDSFYEEHGYLFLRNVLDRDLVKTVAEQMREGLVALGAAD PHATLEELTIDSFESVDEVAMHDYVKYDAFWNNPSTIKVFEQVFGEPVFVFLSTTIRYYP SQAGSEEPSFHYLTPFHQDGFYIGPNQDFRTFWIPLIRTTRESGGVALADGSHRRGKRDH VLNESFRRFGHPVRGIPPTEVSEDEHLLHSPMEPGDILLFHAHMCHKSIPNLSKDPRLMR MSMDTRVQPAKSHRGFNAMTPWTESAKDASKGIMAKITGTPTDVE
- Number of residues
- 285
- Molecular Weight
- 32264.03
- Theoretical pI
- 5.68
- GO Classification
- Functionsiron ion binding / L-ascorbic acid binding / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donorsProcessesantibiotic biosynthetic process / lactone biosynthetic process / oxidation-reduction process
- General Function
- Catalyzes the conversion of 1-deoxypentalenic acid to 11-beta-hydroxy-1-deoxypentalenic acid in the biosynthesis of neopentalenolactone antibiotic.
- Specific Function
- 2-oxoglutarate-dependent dioxygenase activity
- Pfam Domain Function
- PhyH (PF05721)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0012618|1-deoxypentalenic acid 11-beta-hydroxylase (ptlH) GTGACGAACGTGACTGGGGACTACACGGACTGCACTCCTCTGCTCGGCGACCGAGCGGCA CTCGACAGCTTCTACGAGGAACACGGCTACTTATTCCTGCGGAACGTACTCGACCGTGAC CTCGTCAAAACGGTGGCGGAGCAGATGCGGGAAGGACTCGTCGCGCTCGGTGCCGCGGAT CCGCACGCCACGCTCGAGGAACTCACGATCGACTCCTTCGAGTCGGTCGACGAAGTGGCC ATGCACGACTACGTCAAATACGACGCATTCTGGAACAACCCGTCGACCATCAAGGTTTTC GAGCAGGTGTTCGGCGAGCCGGTATTCGTGTTCCTCTCCACGACCATCCGGTACTACCCG TCGCAGGCGGGCTCCGAGGAGCCGTCCTTCCACTACCTGACGCCGTTTCACCAGGACGGC TTCTACATAGGGCCCAACCAGGACTTTCGCACCTTCTGGATCCCCCTGATACGGACGACC AGGGAGTCCGGAGGTGTCGCGCTGGCGGACGGCAGCCACCGGCGCGGAAAGCGCGACCAC GTGCTCAACGAGTCCTTCCGCAGGTTCGGCCACCCGGTGCGCGGAATTCCGCCGACGGAG GTGAGTGAGGACGAACACCTGCTGCACTCCCCCATGGAGCCGGGAGACATCCTCCTCTTT CATGCGCACATGTGCCACAAATCAATTCCGAACCTGTCGAAGGACCCGCGCCTCATGCGG ATGTCGATGGACACCCGGGTACAGCCCGCGAAATCCCACCGCGGCTTCAACGCAATGACG CCCTGGACGGAATCGGCAAAGGACGCGTCAAAGGGAATCATGGCGAAGATCACCGGTACC CCCACCGACGTGGAATGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q82IZ1 UniProtKB Entry Name PTLH_STRAW GenBank Protein ID 29603637 GenBank Gene ID BA000030 PDB ID(s) 2RDN, 2RDQ, 2RDR, 2RDS KEGG ID sma:SAV_2991 - General References
- Omura S, Ikeda H, Ishikawa J, Hanamoto A, Takahashi C, Shinose M, Takahashi Y, Horikawa H, Nakazawa H, Osonoe T, Kikuchi H, Shiba T, Sakaki Y, Hattori M: Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites. Proc Natl Acad Sci U S A. 2001 Oct 9;98(21):12215-20. Epub 2001 Sep 25. [Article]
- Ikeda H, Ishikawa J, Hanamoto A, Shinose M, Kikuchi H, Shiba T, Sakaki Y, Hattori M, Omura S: Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis. Nat Biotechnol. 2003 May;21(5):526-31. Epub 2003 Apr 14. [Article]
- You Z, Omura S, Ikeda H, Cane DE: Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlH, a non-heme iron dioxygenase of Streptomyces avermitilis. J Am Chem Soc. 2006 May 24;128(20):6566-7. [Article]
- Seo MJ, Zhu D, Endo S, Ikeda H, Cane DE: Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the final steps of the biosynthesis of pentalenolactone and neopentalenolactone. Biochemistry. 2011 Mar 15;50(10):1739-54. doi: 10.1021/bi1019786. Epub 2011 Feb 8. [Article]
- You Z, Omura S, Ikeda H, Cane DE, Jogl G: Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis. J Biol Chem. 2007 Dec 14;282(50):36552-60. Epub 2007 Oct 16. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details (1S,3aS,5aR,8aS)-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylic acid experimental unknown target Details