ATP-dependent dethiobiotin synthetase BioD

Details

Name
ATP-dependent dethiobiotin synthetase BioD
Synonyms
  • 6.3.3.3
  • Dethiobiotin synthase
  • DTB synthetase
  • DTBS
Gene Name
bioD
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051231|ATP-dependent dethiobiotin synthetase BioD
MTILVVTGTGTGVGKTVVCAALASAARQAGIDVAVCKPVQTGTARGDDDLAEVGRLAGVT
QLAGLARYPQPMAPAAAAEHAGMALPARDQIVRLIADLDRPGRLTLVEGAGGLLVELAEP
GVTLRDVAVDVAAAALVVVTADLGTLNHTKLTLEALAAQQVSCAGLVIGSWPDPPGLVAA
SNRSALARIAMVRAALPAGAASLDAGDFAAMSAAAFDRNWVAGLVG
Number of residues
226
Molecular Weight
22455.665
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / dethiobiotin synthase activity / magnesium ion binding
Processes
biotin biosynthetic process
Components
cytosol
General 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.
Specific Function
Atp binding
Pfam Domain Function
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0051232|ATP-dependent dethiobiotin synthetase BioD (bioD)
TTGACGATCCTGGTCGTCACCGGGACCGGCACGGGGGTCGGCAAGACGGTCGTCTGCGCG
GCGCTGGCGTCGGCCGCACGTCAGGCCGGCATCGACGTGGCGGTGTGCAAGCCCGTTCAG
ACCGGCACCGCCCGCGGTGACGACGACCTCGCCGAGGTCGGCCGGTTGGCCGGGGTGACC
CAGCTGGCCGGCTTGGCGCGATATCCGCAGCCGATGGCCCCGGCCGCCGCCGCCGAACAC
GCCGGGATGGCGTTGCCCGCCCGCGATCAGATCGTGCGGCTGATCGCAGACCTGGACCGT
CCCGGGCGGTTGACCCTCGTCGAGGGGGCGGGCGGGCTGCTGGTCGAACTCGCCGAGCCG
GGCGTCACGCTGCGCGATGTCGCCGTCGACGTGGCCGCCGCGGCTTTGGTGGTGGTCACC
GCGGACCTGGGCACCCTCAACCACACCAAGTTGACGTTGGAAGCGCTTGCTGCACAACAG
GTTTCATGTGCAGGGCTGGTGATCGGCAGCTGGCCGGACCCGCCCGGGTTGGTGGCAGCC
TCGAATCGGTCCGCGCTGGCGCGCATTGCTATGGTGCGGGCCGCTCTGCCCGCCGGGGCC
GCGTCGCTGGATGCCGGGGACTTCGCGGCGATGAGCGCGGCGGCGTTCGACCGCAACTGG
GTTGCCGGGCTGGTCGGCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WPQ5
UniProtKB Entry NameBIOD_MYCTU
General References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [PubMed:9634230]
  2. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [PubMed:21969609]
  3. Dey S, Lane JM, Lee RE, Rubin EJ, Sacchettini JC: Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase . Biochemistry. 2010 Aug 10;49(31):6746-60. doi: 10.1021/bi902097j. [PubMed:20565114]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03775D-DethiobiotinexperimentalunknownDetails