Name:Molybdopterin synthase sulfur carrier subunit
  • MPT synthase subunit 1
  • Molybdenum cofactor biosynthesis protein D
  • Molybdopterin-converting factor small subunit
  • Molybdopterin-converting factor subunit 1
  • Sulfur carrier protein moaD
Gene Name:moaD
Enzyme Class:Not Available
Biological Properties
General Function:Involved in Mo-molybdopterin cofactor biosynthetic process
Specific Function:Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+2.0Sulfur donor1.0Thumb
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0thiocarboxylated small subunit of molybdopterin synthase4.0Thumb+2.0thiocarboxylated small subunit of molybdopterin synthase+1.0Molybdopterin+1.0Thumb
1.0Cyclic pyranopterin monophosphate + 1.0Water + 1.0thiocarboxylated small subunit of molybdopterin synthase → 4.0Hydrogen ion + 2.0thiocarboxylated small subunit of molybdopterin synthase + 1.0Molybdopterin + 1.0Molybdopterin
Complex Reactions:
1.0Thumb+1.0Thumb+2.0MoaD Protein with thiocarboxylate5.0Thumb+2.0MoaD Protein with carboxylate+1.0Thumb
1.0Cyclic pyranopterin monophosphate + 1.0Copper + 2.0MoaD Protein with thiocarboxylate → 5.0Hydrogen ion + 2.0MoaD Protein with carboxylate + 1.0Molybdopterin
1.0IscS with bound sulfur+1.0MoaD Protein with bound AMP+1.0Thumb1.0Thumb+1.0IscS sulfur acceptor protein+1.0MoaD Protein with thiocarboxylate+1.0Thumb
1.0IscS with bound sulfur + 1.0MoaD Protein with bound AMP + 1.0NADH → 1.0Adenosine monophosphate + 1.0IscS sulfur acceptor protein + 1.0MoaD Protein with thiocarboxylate + 1.0NAD
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB20601Cyclic pyranopterin monophosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
GO Classification:
cellular metabolic process
coenzyme biosynthetic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
Mo-molybdopterin cofactor biosynthetic process
sulfur metabolic process
Gene Properties
Gene OrientationClockwise
Centisome Percentage:17.64
Left Sequence End818271
Right Sequence End818516
Gene Sequence:
>246 bp
Protein Properties
Pfam Domain Function:
Protein Residues:81
Protein Molecular Weight:8758
Protein Theoretical pI:4
PDB File:1JW9
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Molybdopterin synthase sulfur carrier subunit
External Links:
Uniprot ID:P30748
Uniprot Name:MOAD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674470
Ecogene ID:EG11597
Kegg Gene:b0784
EchoBASE ID:EB1554
General Reference:
  • 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
  • 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
  • Lake, M. W., Wuebbens, M. M., Rajagopalan, K. V., Schindelin, H. (2001). "Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex." Nature 414:325-329. Pubmed: 11713534
  • Leimkuhler, S., Wuebbens, M. M., Rajagopalan, K. V. (2001). "Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor." J Biol Chem 276:34695-34701. Pubmed: 11463785
  • 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, a. l. .. (1996). "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 3:137-155. Pubmed: 8905232
  • Pitterle, D. M., Rajagopalan, K. V. (1993). "The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor." J Biol Chem 268:13499-13505. Pubmed: 8514782
  • Rivers, S. L., McNairn, E., Blasco, F., Giordano, G., Boxer, D. H. (1993). "Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis." Mol Microbiol 8:1071-1081. Pubmed: 8361352
  • Rudolph, M. J., Wuebbens, M. M., Rajagopalan, K. V., Schindelin, H. (2001). "Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation." Nat Struct Biol 8:42-46. Pubmed: 11135669
  • Rudolph, M. J., Wuebbens, M. M., Turque, O., Rajagopalan, K. V., Schindelin, H. (2003). "Structural studies of molybdopterin synthase provide insights into its catalytic mechanism." J Biol Chem 278:14514-14522. Pubmed: 12571227
  • Schmitz, J., Wuebbens, M. M., Rajagopalan, K. V., Leimkuhler, S. (2007). "Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold." Biochemistry 46:909-916. Pubmed: 17223713
  • Zhang, W., Urban, A., Mihara, H., Leimkuhler, S., Kurihara, T., Esaki, N. (2010). "IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli." J Biol Chem 285:2302-2308. Pubmed: 19946146