Biotin synthase

Details

Name
Biotin synthase
Synonyms
  • 2.8.1.6
Gene Name
bioB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011235|Biotin synthase
MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYC
PQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGV
KAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKV
RDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDA
FDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDK
DLQLFRKLGLNPQQTAVLAGDNEQQQRLEQALMTPDTDEYYNAAAL
Number of residues
346
Molecular Weight
38647.785
Theoretical pI
5.13
GO Classification
Functions
2 iron, 2 sulfur cluster binding / 4 iron, 4 sulfur cluster binding / biotin synthase activity / iron ion binding
Processes
biotin biosynthetic process
General Function
Iron ion binding
Specific Function
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011236|Biotin synthase (bioB)
ATGGCTCACCGCCCACGCTGGACATTGTCGCAAGTCACAGAATTATTTGAAAAACCGTTG
CTGGATCTGCTGTTTGAAGCGCAGCAGGTGCATCGCCAGCATTTCGATCCTCGTCAGGTG
CAGGTCAGCACGTTGCTGTCGATTAAGACCGGAGCTTGTCCGGAAGATTGCAAATACTGC
CCGCAAAGCTCGCGCTACAAAACCGGGCTGGAAGCCGAGCGGTTGATGGAAGTTGAACAG
GTGCTGGAGTCGGCGCGCAAAGCGAAAGCGGCAGGATCGACGCGCTTCTGTATGGGCGCG
GCGTGGAAGAATCCCCACGAACGCGATATGCCGTACCTGGAACAAATGGTGCAGGGGGTA
AAAGCGATGGGGCTGGAGGCGTGTATGACGCTGGGCACGTTGAGTGAATCTCAGGCGCAG
CGCCTCGCGAACGCCGGGCTGGATTACTACAACCACAACCTGGACACCTCGCCGGAGTTT
TACGGCAATATCATCACCACACGCACTTATCAGGAACGCCTCGATACGCTGGAAAAAGTG
CGCGATGCCGGGATCAAAGTCTGTTCTGGCGGCATTGTGGGCTTAGGCGAAACGGTAAAA
GATCGCGCCGGATTATTGCTGCAACTGGCAAACCTGCCGACGCCGCCGGAAAGCGTGCCA
ATCAACATGCTGGTGAAGGTGAAAGGCACGCCGCTTGCCGATAACGATGATGTCGATGCC
TTTGATTTTATTCGCACCATTGCGGTCGCGCGGATCATGATGCCAACCTCTTACGTGCGC
CTTTCTGCCGGACGCGAGCAGATGAACGAACAGACTCAGGCGATGTGCTTTATGGCAGGC
GCAAACTCGATTTTCTACGGTTGCAAACTGCTGACCACGCCGAATCCGGAAGAAGATAAA
GACCTGCAACTGTTCCGCAAACTGGGGCTAAATCCGCAGCAAACTGCCGTGCTGGCAGGG
GATAACGAACAACAGCAACGTCTTGAACAGGCGCTGATGACCCCGGACACCGACGAATAT
TACAACGCGGCAGCATTATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP12996
UniProtKB Entry NameBIOB_ECOLI
GenBank Protein ID145425
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. 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]
  3. 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]
  4. Sanyal I, Cohen G, Flint DH: Biotin synthase: purification, characterization as a [2Fe-2S]cluster protein, and in vitro activity of the Escherichia coli bioB gene product. Biochemistry. 1994 Mar 29;33(12):3625-31. [Article]
  5. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  6. Farh L, Hwang SY, Steinrauf L, Chiang HJ, Shiuan D: Structure-function studies of Escherichia coli biotin synthase via a chemical modification and site-directed mutagenesis approach. J Biochem. 2001 Nov;130(5):627-35. [Article]
  7. Cosper MM, Jameson GN, Davydov R, Eidsness MK, Hoffman BM, Huynh BH, Johnson MK: The [4Fe-4S](2+) cluster in reconstituted biotin synthase binds S-adenosyl-L-methionine. J Am Chem Soc. 2002 Nov 27;124(47):14006-7. [Article]
  8. Ollagnier-de Choudens S, Sanakis Y, Hewitson KS, Roach P, Munck E, Fontecave M: Reductive cleavage of S-adenosylmethionine by biotin synthase from Escherichia coli. J Biol Chem. 2002 Apr 19;277(16):13449-54. Epub 2002 Feb 7. [Article]
  9. Hewitson KS, Ollagnier-de Choudens S, Sanakis Y, Shaw NM, Baldwin JE, Munck E, Roach PL, Fontecave M: The iron-sulfur center of biotin synthase: site-directed mutants. J Biol Inorg Chem. 2002 Jan;7(1-2):83-93. Epub 2001 Jul 11. [Article]
  10. Cosper MM, Cosper NJ, Hong W, Shokes JE, Broderick WE, Broderick JB, Johnson MK, Scott RA: Structural studies of the interaction of S-adenosylmethionine with the [4Fe-4S] clusters in biotin synthase and pyruvate formate-lyase activating enzyme. Protein Sci. 2003 Jul;12(7):1573-7. [Article]
  11. Lotierzo M, Bui BT, Leech HK, Warren MJ, Marquet A, Rigby SE: Iron-sulfur cluster dynamics in biotin synthase: a new [2Fe-2S](1+) cluster. Biochem Biophys Res Commun. 2009 Apr 17;381(4):487-90. doi: 10.1016/j.bbrc.2009.02.089. Epub 2009 Feb 24. [Article]
  12. Lotierzo M, Raux E, Tse Sum Bui B, Goasdoue N, Libot F, Florentin D, Warren MJ, Marquet A: Biotin synthase mechanism: mutagenesis of the YNHNLD conserved motif. Biochemistry. 2006 Oct 10;45(40):12274-81. [Article]
  13. Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL: Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science. 2004 Jan 2;303(5654):76-9. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03775DethiobiotinexperimentalunknownDetails