Biotin synthase (P12996)

Identification
Name:Biotin synthase
Synonyms:Not Available
Gene Name:bioB
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical- based mechanism
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Sulfur donor+2.0Thumb+2.0e-+2.0Thumb ↔ 1.0Thumb+2.0Thumb+2.0Thumb
1.0Dethiobiotin + 1.0Sulfur donor + 2.0S-Adenosylmethionine + 2.0e- + 2.0Hydrogen ion ↔ 1.0Biotin + 2.0L-Methionine + 2.05'-Deoxyadenosine
ReactionCard
SMPDB Reactions:
1.0Thumb+2.0S-adenosyl-L-methionine+2.0Thumb+1.0Thumb → 1.0Thumb+2.0Thumb+2.0Thumb
1.0Dethiobiotin + 2.0S-adenosyl-L-methionine + 2.0Hydrogen ion + 1.0a sulfurated [sulfur carrier] → 1.0Biotin + 2.0L-Methionine + 2.05'-Deoxyadenosine
ReactionCard
Complex Reactions:
1.0[2Fe-2S] iron-sulfur cluster+1.0Thumb+1.0Thumb → 1.0[2Fe-1S] desulfurated iron-sulfur cluster+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0[2Fe-2S] iron-sulfur cluster + 1.0S-Adenosylmethionine + 1.0Dethiobiotin → 1.0[2Fe-1S] desulfurated iron-sulfur cluster + 1.0Biotin + 1.05'-Deoxyadenosine + 1.0Hydrogen ion + 1.0L-Methionine
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211745'-DeoxyadenosineMetaboCard
ECMDB24186a sulfurated [sulfur carrier]MetaboCard
ECMDB00030BiotinMetaboCard
ECMDB03581DethiobiotinMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB03276Hydrogen sulfideMetaboCard
ECMDB00696L-MethionineMetaboCard
ECMDB01185S-AdenosylmethionineMetaboCard
GO Classification:
Function
binding
biotin synthase activity
catalytic activity
iron-sulfur cluster binding
metal cluster binding
sulfurtransferase activity
transferase activity
transferase activity, transferring sulfur-containing groups
Process
biotin biosynthetic process
biotin metabolic process
cellular metabolic process
cofactor metabolic process
metabolic process
small molecule metabolic process
vitamin metabolic process
water-soluble vitamin metabolic process
Gene Properties
Blattner:b0775
Gene OrientationClockwise
Centisome Percentage:17.43
Left Sequence End808567
Right Sequence End809607
Gene Sequence:
>1041 bp
ATGGCTCACCGCCCACGCTGGACATTGTCGCAAGTCACAGAATTATTTGAAAAACCGTTG
CTGGATCTGCTGTTTGAAGCGCAGCAGGTGCATCGCCAGCATTTCGATCCTCGTCAGGTG
CAGGTCAGCACGTTGCTGTCGATTAAGACCGGAGCTTGTCCGGAAGATTGCAAATACTGC
CCGCAAAGCTCGCGCTACAAAACCGGGCTGGAAGCCGAGCGGTTGATGGAAGTTGAACAG
GTGCTGGAGTCGGCGCGCAAAGCGAAAGCGGCAGGATCGACGCGCTTCTGTATGGGCGCG
GCGTGGAAGAATCCCCACGAACGCGATATGCCGTACCTGGAACAAATGGTGCAGGGGGTA
AAAGCGATGGGGCTGGAGGCGTGTATGACGCTGGGCACGTTGAGTGAATCTCAGGCGCAG
CGCCTCGCGAACGCCGGGCTGGATTACTACAACCACAACCTGGACACCTCGCCGGAGTTT
TACGGCAATATCATCACCACACGCACTTATCAGGAACGCCTCGATACGCTGGAAAAAGTG
CGCGATGCCGGGATCAAAGTCTGTTCTGGCGGCATTGTGGGCTTAGGCGAAACGGTAAAA
GATCGCGCCGGATTATTGCTGCAACTGGCAAACCTGCCGACGCCGCCGGAAAGCGTGCCA
ATCAACATGCTGGTGAAGGTGAAAGGCACGCCGCTTGCCGATAACGATGATGTCGATGCC
TTTGATTTTATTCGCACCATTGCGGTCGCGCGGATCATGATGCCAACCTCTTACGTGCGC
CTTTCTGCCGGACGCGAGCAGATGAACGAACAGACTCAGGCGATGTGCTTTATGGCAGGC
GCAAACTCGATTTTCTACGGTTGCAAACTGCTGACCACGCCGAATCCGGAAGAAGATAAA
GACCTGCAACTGTTCCGCAAACTGGGGCTAAATCCGCAGCAAACTGCCGTGCTGGCAGGG
GATAACGAACAACAGCAACGTCTTGAACAGGCGCTGATGACCCCGGACACCGACGAATAT
TACAACGCGGCAGCATTATGA
Protein Properties
Pfam Domain Function:
Protein Residues:346
Protein Molecular Weight:38648
Protein Theoretical pI:5
PDB File:1R30
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Biotin synthase
MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYC
PQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGV
KAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKV
RDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDA
FDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDK
DLQLFRKLGLNPQQTAVLAGDNEQQQRLEQALMTPDTDEYYNAAAL
References
External Links:
ResourceLink
Uniprot ID:P12996
Uniprot Name:BIOB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674758
PDB ID:1R30
Ecogene ID:EG10118
Ecocyc:EG10118
ColiBase:b0775
Kegg Gene:b0775
EchoBASE ID:EB0116
CCDB:BIOB_ECOLI
BacMap:16128743
General Reference:
  • Berkovitch, F., Nicolet, Y., Wan, J. T., Jarrett, J. T., Drennan, C. L. (2004). "Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme." Science 303:76-79. Pubmed: 14704425
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Cosper, M. M., Cosper, N. J., Hong, W., Shokes, J. E., Broderick, W. E., Broderick, J. B., Johnson, M. K., Scott, R. A. (2003). "Structural studies of the interaction of S-adenosylmethionine with the [4Fe-4S] clusters in biotin synthase and pyruvate formate-lyase activating enzyme." Protein Sci 12:1573-1577. Pubmed: 12824504
  • Cosper, M. M., Jameson, G. N., Davydov, R., Eidsness, M. K., Hoffman, B. M., Huynh, B. H., Johnson, M. K. (2002). "The [4Fe-4S](2+) cluster in reconstituted biotin synthase binds S-adenosyl-L-methionine." J Am Chem Soc 124:14006-14007. Pubmed: 12440894
  • Farh, L., Hwang, S. Y., Steinrauf, L., Chiang, H. J., Shiuan, D. (2001). "Structure-function studies of Escherichia coli biotin synthase via a chemical modification and site-directed mutagenesis approach." J Biochem 130:627-635. Pubmed: 11686925
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Hewitson, K. S., Ollagnier-de Choudens, S., Sanakis, Y., Shaw, N. M., Baldwin, J. E., Munck, E., Roach, P. L., Fontecave, M. (2002). "The iron-sulfur center of biotin synthase: site-directed mutants." J Biol Inorg Chem 7:83-93. Pubmed: 11862544
  • Lotierzo, M., Bui, B. T., Leech, H. K., Warren, M. J., Marquet, A., Rigby, S. E. (2009). "Iron-sulfur cluster dynamics in biotin synthase: a new [2Fe-2S](1+) cluster." Biochem Biophys Res Commun 381:487-490. Pubmed: 19245793
  • Lotierzo, M., Raux, E., Tse Sum Bui, B., Goasdoue, N., Libot, F., Florentin, D., Warren, M. J., Marquet, A. (2006). "Biotin synthase mechanism: mutagenesis of the YNHNLD conserved motif." Biochemistry 45:12274-12281. Pubmed: 17014080
  • Ollagnier-de Choudens, S., Sanakis, Y., Hewitson, K. S., Roach, P., Munck, E., Fontecave, M. (2002). "Reductive cleavage of S-adenosylmethionine by biotin synthase from Escherichia coli." J Biol Chem 277:13449-13454. Pubmed: 11834738
  • Otsuka, A. J., Buoncristiani, M. R., Howard, P. K., Flamm, J., Johnson, C., Yamamoto, R., Uchida, K., Cook, C., Ruppert, J., Matsuzaki, J. (1988). "The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon." J Biol Chem 263:19577-19585. Pubmed: 3058702
  • Sanyal, I., Cohen, G., Flint, D. H. (1994). "Biotin synthase: purification, characterization as a [2Fe-2S]cluster protein, and in vitro activity of the Escherichia coli bioB gene product." Biochemistry 33:3625-3631. Pubmed: 8142361