Pyridoxine 5'-phosphate synthase
Details
- Name
- Pyridoxine 5'-phosphate synthase
- Synonyms
- 2.6.99.2
- PNP synthase
- Gene Name
- pdxJ
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0003058|Pyridoxine 5'-phosphate synthase MAELLLGVNIDHIATLRNARGTAYPDPVQAAFIAEQAGADGITVHLREDRRHITDRDVRI LRQTLDTRMNLEMAVTEEMLAIAVETKPHFCCLVPEKRQEVTTEGGLDVAGQRDKMRDAC KRLADAGIQVSLFIDADEEQIKAAAEVGAPFIEIHTGCYADAKTDAEQAQELARIAKAAT FAASLGLKVNAGHGLTYHNVKAIAAIPEMHELNIGHAIIGRAVMTGLKDAVAEMKRLMLE ARG
- Number of residues
- 243
- Molecular Weight
- 26384.01
- Theoretical pI
- 5.82
- GO Classification
- Functionspyridoxine 5'-phosphate synthase activityProcessespyridoxine biosynthetic processComponentscytosol
- General Function
- Pyridoxine 5'-phosphate synthase activity
- Specific Function
- Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
- Pfam Domain Function
- PdxJ (PF03740)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0011091|Pyridoxine 5'-phosphate synthase (pdxJ) ATGGCTGAATTACTGTTAGGCGTCAACATTGACCATATCGCTACGCTGCGCAACGCGCGC GGTACCGCTTACCCGGATCCGGTGCAGGCCGCGTTTATTGCCGAGCAGGCGGGAGCGGAC GGCATTACCGTGCATTTACGTGAAGATCGCCGTCACATTACTGACCGCGACGTGCGCATC CTGCGTCAGACGCTGGATACCCGCATGAATCTGGAGATGGCGGTGACCGAAGAGATGCTG GCGATCGCCGTTGAGACGAAGCCACATTTTTGCTGCCTGGTACCGGAAAAGCGTCAGGAA GTAACAACCGAAGGCGGCCTGGATGTCGCAGGGCAGCGTGACAAAATGCGCGATGCCTGC AAACGTCTGGCAGATGCCGGGATTCAGGTTTCTCTGTTTATTGACGCCGATGAAGAGCAG ATCAAAGCTGCGGCAGAGGTTGGCGCACCGTTTATCGAGATCCACACCGGTTGCTATGCT GATGCCAAAACTGACGCCGAACAGGCGCAAGAGCTGGCGCGTATCGCCAAAGCCGCGACC TTTGCCGCAAGCCTCGGTCTGAAAGTTAACGCCGGACACGGTCTGACCTATCACAACGTG AAAGCCATTGCCGCCATCCCTGAGATGCATGAACTGAATATCGGTCATGCCATTATTGGT CGTGCAGTGATGACCGGACTGAAAGATGCGGTGGCAGAAATGAAGCGTCTGATGCTGGAA GCGCGTGGCTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A794 UniProtKB Entry Name PDXJ_ECOLI GenBank Protein ID 147555 GenBank Gene ID M76470 - General References
- Takiff HE, Baker T, Copeland T, Chen SM, Court DL: Locating essential Escherichia coli genes by using mini-Tn10 transposons: the pdxJ operon. J Bacteriol. 1992 Mar;174(5):1544-53. [Article]
- Lam HM, Tancula E, Dempsey WB, Winkler ME: Suppression of insertions in the complex pdxJ operon of Escherichia coli K-12 by lon and other mutations. J Bacteriol. 1992 Mar;174(5):1554-67. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Man TK, Zhao G, Winkler ME: Isolation of a pdxJ point mutation that bypasses the requirement for the PdxH oxidase in pyridoxal 5' -phosphate coenzyme biosynthesis in Escherichia coli K-12. J Bacteriol. 1996 Apr;178(8):2445-9. [Article]
- Laber B, Maurer W, Scharf S, Stepusin K, Schmidt FS: Vitamin B6 biosynthesis: formation of pyridoxine 5'-phosphate from 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by PdxA and PdxJ protein. FEBS Lett. 1999 Apr 16;449(1):45-8. [Article]
- Garrido Franco M, Huber R, Schmidt FS, Laber B, Clausen T: Crystallization and preliminary X-ray crystallographic analysis of PdxJ, the pyridoxine 5'-phosphate synthesizing enzyme. Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):1045-8. [Article]
- Garrido-Franco M: Pyridoxine 5'-phosphate synthase: de novo synthesis of vitamin B6 and beyond. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):92-7. [Article]
- Franco MG, Laber B, Huber R, Clausen T: Structural basis for the function of pyridoxine 5'-phosphate synthase. Structure. 2001 Mar 7;9(3):245-53. [Article]
- Yeh JI, Du S, Pohl E, Cane DE: Multistate binding in pyridoxine 5'-phosphate synthase: 1.96 A crystal structure in complex with 1-deoxy-D-xylulose phosphate. Biochemistry. 2002 Oct 1;41(39):11649-57. [Article]
- Garrido-Franco M, Laber B, Huber R, Clausen T: Enzyme-ligand complexes of pyridoxine 5'-phosphate synthase: implications for substrate binding and catalysis. J Mol Biol. 2002 Aug 23;321(4):601-12. [Article]