Identification
Name:Sulfur carrier protein moaD adenylyltransferase
Synonyms:
  • MoaD protein adenylase
  • Molybdopterin-converting factor subunit 1 adenylase
Gene Name:moeB
Enzyme Class:Not Available
Biological Properties
General Function:Involved in Mo-molybdopterin cofactor biosynthetic process
Specific Function:Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein moaD
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:
Complex Reactions:
1.0Thumb+1.0Thumb+1.0MoaD Protein with carboxylate1.0MoaD Protein with bound AMP+1.0Thumb
1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0MoaD Protein with carboxylate → 1.0MoaD Protein with bound AMP + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly1.0Thumb+1.0[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP
1.0Adenosine triphosphate + 1.0[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly → 1.0Pyrophosphate + 1.0[molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Function
binding
catalytic activity
Process
cellular metabolic process
coenzyme biosynthetic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
Mo-molybdopterin cofactor biosynthetic process
Gene Properties
Blattner:b0826
Gene OrientationCounterclockwise
Centisome Percentage:18.61
Left Sequence End863603
Right Sequence End864352
Gene Sequence:
>750 bp
ATGTCCTTGCCGTCGATTCCATCCTTTGTATTGTCGGGATTACTGTTGATTTGTTTGCCG
TTTTCTTCATTTGCCAGCGCCACCACATCACATATCTCTTTCAGCTACGCCGCCCGCCAG
CGGATGCAAAACCGTGCGCGTTTATTAAAACAGTACCAAACTCATCTGAAAAAGCAGGCC
AGCTATATTGTGGAAGGCAATGCCGAAAGCAAAAGGGCGCTACGCCAGCACAACCGGGAG
CAGATAAAACAGCATCCAGAATGGTTTCCTGCTCCGCTCAAGGCGAGTGACAGACGCTGG
CAGGCGCTGGCGGAAAACAACCACTTTTTAAGCAGCGACCATCTGCATAACATTACCGAA
GTGGCGATTCACCGCCTGGAGCAGCAGCTTGGCAAGCCTTACGTCTGGGGCGGTACGCGG
CCTGATAAAGGCTTTGACTGTAGCGGGTTGGTTTTTTATGCCTACAACAAGATCCTTGAG
GCTAAGCTCCCGCGCACGGCCAATGAGATGTACCACTATCGCCGGGCAACGATTGTGGCG
AACAACGACCTGCGCCGGGGAGATTTGCTGTTTTTCCATATCCACAGCCGCGAGATAGCC
GATCATATGGGCGTGTATTTGGGCGATGGGCAATTTATCGAGTCGCCACGTACCGGCGAA
ACCATTCGGATAAGCCGATTAGCCGAACCTTTCTGGCAGGACCATTTTTTGGGCGCGCGC
AGGATTTTGACGGAAGAGACGATTTTGTAG
Protein Properties
Pfam Domain Function:
Protein Residues:249
Protein Molecular Weight:26719
Protein Theoretical pI:5
PDB File:1JW9
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Sulfur carrier protein moaD adenylyltransferase
MAELSDQEMLRYNRQIILRGFDFDGQEALKDSRVLIVGLGGLGCAASQYLASAGVGNLTL
LDFDTVSLSNLQRQTLHSDATVGQPKVESARDALTRINPHIAITPVNALLDDAELAALIA
EHDLVLDCTDNVAVRNQLNAGCFAAKVPLVSGAAIRMEGQITVFTYQDGEPCYRCLSRLF
GENALTCVEAGVMAPLIGVIGSLQAMEAIKMLAGYGKPASGKIVMYDAMTCQFREMKLMR
NPGCEVCGQ
References
External Links:
ResourceLink
Uniprot ID:P12282
Uniprot Name:MOEB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674388
PDB ID:1JW9
Ecogene ID:EG10154
Ecocyc:EG10154
ColiBase:b0826
Kegg Gene:b0826
EchoBASE ID:EB0152
CCDB:MOEB_ECOLI
BacMap:16128794
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., Rajagopalan, K. V. (2001). "A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli." J Biol Chem 276:22024-22031. Pubmed: 11290749
  • 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
  • Nohno, T., Kasai, Y., Saito, T. (1988). "Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis." J Bacteriol 170:4097-4102. Pubmed: 3045084
  • 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