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
- Functionsmolybdopterin synthase activityProcessesMo-molybdopterin cofactor biosynthetic process / molybdopterin cofactor biosynthetic processComponentscytosol
- 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
- MoaE (PF02391)
- 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
Resource Link UniProtKB ID P30749 UniProtKB Entry Name MOAE_ECOLI GenBank Gene ID X70420 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]