ATP-dependent dethiobiotin synthetase BioD 1

Details

Name
ATP-dependent dethiobiotin synthetase BioD 1
Synonyms
  • 6.3.3.3
  • Dethiobiotin synthase
  • DTB synthetase 1
  • DTBS 1
Gene Name
bioD1
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0010885|ATP-dependent dethiobiotin synthetase BioD 1
MSKRYFVTGTDTEVGKTVASCALLQAAKAAGYRTAGYKPVASGSEKTPEGLRNSDALALQ
RNSSLQLDYATVNPYTFAEPTSPHIISAQEGRPIESLVMSAGLRALEQQADWVLVEGAGG
WFTPLSDTFTFADWVTQEQLPVILVVGVKLGCINHAMLTAQVIQHAGLTLAGWVANDVTP
PGKRHAEYMTTLTRMIPAPLLGEIPWLAENPENAATGKYINLALL
Number of residues
225
Molecular Weight
24139.38
Theoretical pI
5.64
GO Classification
Functions
ATP binding / dethiobiotin synthase activity / magnesium ion binding
Processes
biotin biosynthetic process
Components
cytosol
General Function
Magnesium ion binding
Specific Function
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. Only CTP can partially replace ATP while diaminobiotin is only 37% as effective as 7,8-diaminopelargonic acid.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0010886|ATP-dependent dethiobiotin synthetase BioD 1 (bioD1)
GTGAGTAAACGTTATTTTGTCACCGGAACGGATACCGAAGTGGGGAAAACTGTCGCCAGT
TGTGCACTTTTACAAGCCGCAAAGGCAGCAGGCTACCGGACGGCAGGTTATAAACCGGTC
GCCTCTGGCAGCGAAAAGACCCCGGAAGGTTTACGCAATAGCGACGCGCTGGCGTTACAG
CGCAACAGCAGCCTGCAGCTGGATTACGCAACAGTAAATCCTTACACCTTCGCAGAACCC
ACTTCGCCGCACATCATCAGCGCGCAAGAGGGCAGACCGATAGAATCATTGGTAATGAGC
GCCGGATTACGCGCGCTTGAACAACAGGCTGACTGGGTGTTAGTGGAAGGTGCTGGCGGC
TGGTTTACGCCGCTTTCTGACACTTTCACTTTTGCAGATTGGGTAACACAGGAACAACTG
CCGGTGATACTGGTAGTTGGTGTGAAACTCGGCTGTATTAATCACGCGATGTTGACTGCA
CAGGTAATACAACACGCCGGACTGACTCTGGCGGGTTGGGTGGCGAACGATGTTACGCCT
CCGGGAAAACGTCACGCTGAATATATGACCACGCTCACCCGCATGATTCCCGCGCCGCTG
CTGGGAGAGATCCCCTGGCTTGCAGAAAATCCAGAAAATGCGGCAACCGGAAAGTACATA
AACCTTGCCTTGTTGTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP13000
UniProtKB Entry NameBIOD1_ECOLI
GenBank Protein ID145427
GenBank Gene IDJ04423
General References
  1. Otsuka AJ, Buoncristiani MR, Howard PK, Flamm J, Johnson C, Yamamoto R, Uchida K, Cook C, Ruppert J, Matsuzaki J: The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon. J Biol Chem. 1988 Dec 25;263(36):19577-85. [Article]
  2. Alexeev D, Bury SM, Boys CW, Turner MA, Sawyer L, Ramsey AJ, Baxter HC, Baxter RL: Sequence and crystallization of Escherichia coli dethiobiotin synthetase, the penultimate enzyme of biotin biosynthesis. J Mol Biol. 1994 Jan 14;235(2):774-6. [Article]
  3. 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]
  4. 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]
  5. Eisenberg MA, Krell K: Synthesis of desthiobiotin from 7,8-diaminopelargonic acid in biotin auxotrophs of Escherichia coli K-12. J Bacteriol. 1969 Jun;98(3):1227-31. [Article]
  6. Krell K, Eisenberg MA: The purification and properties of dethiobiotin synthetase. J Biol Chem. 1970 Dec 25;245(24):6558-66. [Article]
  7. Yang G, Sandalova T, Lohman K, Lindqvist Y, Rendina AR: Active site mutants of Escherichia coli dethiobiotin synthetase: effects of mutations on enzyme catalytic and structural properties. Biochemistry. 1997 Apr 22;36(16):4751-60. [Article]
  8. Huang W, Lindqvist Y, Schneider G, Gibson KJ, Flint D, Lorimer G: Crystal structure of an ATP-dependent carboxylase, dethiobiotin synthetase, at 1.65 A resolution. Structure. 1994 May 15;2(5):407-14. [Article]
  9. Alexeev D, Baxter RL, Sawyer L: Mechanistic implications and family relationships from the structure of dethiobiotin synthetase. Structure. 1994 Nov 15;2(11):1061-72. [Article]
  10. Huang W, Jia J, Gibson KJ, Taylor WS, Rendina AR, Schneider G, Lindqvist Y: Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based on crystallographic studies of complexes with substrates and a reaction intermediate. Biochemistry. 1995 Sep 5;34(35):10985-95. [Article]
  11. Kack H, Gibson KJ, Lindqvist Y, Schneider G: Snapshot of a phosphorylated substrate intermediate by kinetic crystallography. Proc Natl Acad Sci U S A. 1998 May 12;95(10):5495-500. [Article]
  12. Kack H, Sandmark J, Gibson KJ, Schneider G, Lindqvist Y: Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis. Protein Sci. 1998 Dec;7(12):2560-6. [Article]
  13. Sandalova T, Schneider G, Kack H, Lindqvist Y: Structure of dethiobiotin synthetase at 0.97 A resolution. Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):610-24. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB017157,8-Diamino-Nonanoic AcidexperimentalunknownDetails
DB02927Mixed Carbamic Phosphoric Acid Anhydride of 7,8-Diaminononanic AcidexperimentalunknownDetails
DB029413-(1-Aminoethyl)Nonanedioic AcidexperimentalunknownDetails
DB036247-(Carboxyamino)-8-Amino-Nonanoic AcidexperimentalunknownDetails
DB03775DethiobiotinexperimentalunknownDetails