Molybdopterin molybdenumtransferase (P12281)

Identification
Name:Molybdopterin molybdenumtransferase
Synonyms:
  • MPT Mo-transferase
Gene Name:moeA
Enzyme Class:
Biological Properties
General Function:Involved in Mo-molybdopterin cofactor biosynthetic process
Specific Function:Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:Not Available
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Molybdoenzyme molybdenum cofactor+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenylated molybdopterin + 1.0Molybdate ↔ 1.0Molybdoenzyme molybdenum cofactor + 1.0Adenosine monophosphate + 1.0Water + 1.0Molybdoenzyme molybdenum cofactor
ReactionCard
SMPDB Reactions:
1.0Adenylyl-molybdopterin+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenylyl-molybdopterin + 1.0Hydrogen ion + 1.0Molybdate → 1.0Adenosine monophosphate + 1.0Water + 1.0molybdenum cofactor
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0molybdenum cofactor+1.0Thumb+1.0Thumb
1.0Adenylated molybdopterin + 1.0Molybdate → 1.0molybdenum cofactor + 1.0Adenosine monophosphate + 1.0Water
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0bis-molybdenum cofactor+1.0Thumb
1.0Molybdopterin + 1.0Adenylated molybdopterin → 1.0Adenosine monophosphate + 1.0bis-molybdenum cofactor + 1.0Copper
ReactionCard
1.0Thumb+1.0tungsten binding cofactor → 1.0Thumb+1.0tungsten bispterin cofactor+1.0Thumb
1.0Adenylated molybdopterin + 1.0tungsten binding cofactor → 1.0Adenosine monophosphate + 1.0tungsten bispterin cofactor + 1.0Copper
ReactionCard
2.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
2.0Hydrogen ion + 1.0Molybdate + 1.0Adenylated molybdopterin → 1.0Adenosine monophosphate + 1.0Copper + 1.0Water + 1.0Molybdopterin
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB21307Adenylated molybdopterinMetaboCard
ECMDB00657CopperMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21246MolybdateMetaboCard
ECMDB23236molybdenum cofactorMetaboCard
ECMDB23792Molybdoenzyme molybdenum cofactorMetaboCard
ECMDB02206MolybdopterinMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Process
biosynthetic process
cellular biosynthetic process
cellular metabolic process
coenzyme biosynthetic process
coenzyme metabolic process
cofactor metabolic process
heterocycle biosynthetic process
metabolic process
Mo-molybdopterin cofactor biosynthetic process
molybdopterin cofactor biosynthetic process
pteridine and derivative biosynthetic process
Gene Properties
Blattner:b0827
Gene OrientationCounterclockwise
Centisome Percentage:18.63
Left Sequence End864352
Right Sequence End865587
Gene Sequence:
>1236 bp
ATGGAATTTACCACCGGATTGATGTCGCTCGACACCGCGCTTAATGAGATGCTTTCTCGC
GTCACCCCACTGACCGCCCAGGAAACGCTGCCACTGGTACAGTGTTTTGGTCGTATTCTG
GCGAGCGATGTCGTTTCGCCGCTTGATGTTCCGGGGTTTGATAACTCCGCAATGGACGGC
TACGCGGTGCGTTTAGCCGATATTGCCTCCGGGCAACCGCTGCCCGTTGCCGGTAAATCC
TTTGCCGGTCAGCCATACCATGGTGAATGGCCTGCGGGTACCTGCATTCGTATTATGACC
GGTGCGCCGGTGCCGGAAGGCTGCGAAGCGGTGGTGATGCAGGAGCAGACTGAACAAATG
GACAATGGCGTGCGTTTTACTGCTGAAGTGCGTAGCGGGCAAAATATTCGCCGTCGCGGT
GAAGATATCTCTGCAGGTGCGGTTGTTTTCCCGGCGGGAACTCGCCTGACTACCGCAGAG
CTGCCAGTAATTGCTTCACTGGGGATTGCCGAAGTTCCGGTGATTCGTAAAGTGCGTGTA
GCGCTTTTTTCTACCGGTGATGAACTCCAGTTGCCCGGTCAGCCGCTGGGCGACGGCCAA
ATCTACGATACCAACCGTCTCGCCGTACACCTGATGTTAGAACAGTTGGGATGCGAGGTA
ATTAACTTAGGGATTATCCGCGACGATCCCCATGCCCTGCGCGCCGCATTTATTGAAGCC
GACAGCCAGGCGGATGTGGTGATCAGTTCCGGCGGTGTTTCAGTGGGTGAGGCGGATTAC
ACCAAAACGATTCTTGAAGAGCTGGGGGAGATCGCCTTCTGGAAGCTGGCGATTAAACCA
GGTAAACCGTTCGCGTTCGGTAAACTCAGCAATAGCTGGTTCTGCGGCCTGCCGGGCAAC
CCGGTTTCAGCGACGCTGACCTTCTATCAACTGGTACAGCCTTTGCTGGCAAAACTAAGC
GGTAACACCGCCAGCGGCCTGCCCGCGCGCCAGCGCGTACGCACAGCGTCCCGCCTGAAA
AAAACGCCAGGACGTCTTGATTTCCAGCGCGGCGTGCTGCAACGCAACGCCGATGGCGAA
CTGGAAGTGACGACCACCGGACATCAGGGTTCACATATATTTAGCTCCTTTAGCCTCGGC
AACTGCTTTATCGTGCTGGAACGCGATCGCGGCAATGTGGAAGTGGGCGAATGGGTGGAA
GTAGAACCGTTTAACGCGTTGTTCGGAGGCCTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:411
Protein Molecular Weight:44067
Protein Theoretical pI:5
PDB File:1G8R
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Molybdopterin molybdenumtransferase
MEFTTGLMSLDTALNEMLSRVTPLTAQETLPLVQCFGRILASDVVSPLDVPGFDNSAMDG
YAVRLADIASGQPLPVAGKSFAGQPYHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQM
DNGVRFTAEVRSGQNIRRRGEDISAGAVVFPAGTRLTTAELPVIASLGIAEVPVIRKVRV
ALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEA
DSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGN
PVSATLTFYQLVQPLLAKLSGNTASGLPARQRVRTASRLKKTPGRLDFQRGVLQRNADGE
LEVTTTGHQGSHIFSSFSLGNCFIVLERDRGNVEVGEWVEVEPFNALFGGL
References
External Links:
ResourceLink
Uniprot ID:P12281
Uniprot Name:MOEA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651376
PDB ID:1G8R
Ecogene ID:EG10153
Ecocyc:EG10153
ColiBase:b0827
Kegg Gene:b0827
EchoBASE ID:EB0151
CCDB:MOEA_ECOLI
BacMap:16128795
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
  • Hasona, A., Ray, R. M., Shanmugam, K. T. (1998). "Physiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coli." J Bacteriol 180:1466-1472. Pubmed: 9515915
  • 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
  • Nichols, J. D., Rajagopalan, K. V. (2005). "In vitro molybdenum ligation to molybdopterin using purified components." J Biol Chem 280:7817-7822. Pubmed: 15632135
  • 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
  • Schrag, J. D., Huang, W., Sivaraman, J., Smith, C., Plamondon, J., Larocque, R., Matte, A., Cygler, M. (2001). "The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway." J Mol Biol 310:419-431. Pubmed: 11428898
  • Xiang, S., Nichols, J., Rajagopalan, K. V., Schindelin, H. (2001). "The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin." Structure 9:299-310. Pubmed: 11525167