Molybdopterin synthase catalytic subunit

Details

Name
Molybdopterin synthase catalytic subunit
Synonyms
  • 2.8.1.12
  • chlA5
  • Molybdenum cofactor biosynthesis protein E
  • Molybdopterin-converting factor large subunit
  • Molybdopterin-converting factor subunit 2
  • MPT synthase subunit 2
Gene Name
moaE
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011886|Molybdopterin synthase catalytic subunit
MAETKIVVGPQPFSVGEEYPWLAERDEDGAVVTFTGKVRNHNLGDSVNALTLEHYPGMTE
KALAEIVDEARNRWPLGRVTVIHRIGELWPGDEIVFVGVTSAHRSSAFEAGQFIMDYLKT
RAPFWKREATPEGDRWVEARESDQQAAKRW
Number of residues
150
Molecular Weight
16980.955
Theoretical pI
5.06
GO Classification
Functions
molybdopterin synthase activity
Processes
Mo-molybdopterin cofactor biosynthetic process / molybdopterin cofactor biosynthetic process
Components
cytosol
General Function
Molybdopterin synthase activity
Specific Function
Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011887|Molybdopterin synthase catalytic subunit (moaE)
ATGGCAGAAACCAAAATTGTTGTTGGTCCGCAGCCGTTCAGCGTAGGAGAAGAGTACCCG
TGGCTGGCGGAGCGTGACGAAGACGGTGCGGTAGTCACCTTTACTGGTAAGGTGCGCAAC
CATAACCTGGGCGACAGCGTCAACGCATTAACCCTCGAACACTATCCGGGGATGACTGAA
AAAGCACTGGCAGAAATTGTTGATGAAGCGCGTAACCGCTGGCCGCTGGGGCGCGTCACT
GTGATTCACCGCATCGGGGAATTATGGCCGGGCGATGAAATCGTTTTTGTCGGTGTCACC
AGTGCGCATCGCAGCAGTGCGTTTGAAGCCGGGCAGTTTATTATGGATTATCTCAAAACC
CGCGCACCGTTCTGGAAGCGCGAAGCCACGCCGGAAGGCGACCGCTGGGTTGAAGCTCGG
GAGAGCGATCAGCAGGCGGCAAAACGCTGGTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP30749
UniProtKB Entry NameMOAE_ECOLI
GenBank Gene IDX70420
General References
  1. Rivers SL, McNairn E, Blasco F, Giordano G, Boxer DH: Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis. Mol Microbiol. 1993 Jun;8(6):1071-81. [Article]
  2. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [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. Pitterle DM, Rajagopalan KV: The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor. J Biol Chem. 1993 Jun 25;268(18):13499-505. [Article]
  6. Wuebbens MM, Rajagopalan KV: Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis. J Biol Chem. 2003 Apr 18;278(16):14523-32. Epub 2003 Feb 5. [Article]
  7. Rudolph MJ, Wuebbens MM, Rajagopalan KV, Schindelin H: Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat Struct Biol. 2001 Jan;8(1):42-6. [Article]
  8. Rudolph MJ, Wuebbens MM, Turque O, Rajagopalan KV, Schindelin H: Structural studies of molybdopterin synthase provide insights into its catalytic mechanism. J Biol Chem. 2003 Apr 18;278(16):14514-22. Epub 2003 Feb 5. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01942Formic acidexperimental, investigationalunknownDetails