Molybdenum cofactor guanylyltransferase

NameMolybdenum cofactor guanylyltransferase
Synonyms
  • 2.7.7.77
  • chlB
  • GTP:molybdopterin guanylyltransferase
  • MGD synthase
  • Mo-MPT guanylyltransferase
  • mob
  • MoCo guanylyltransferase
  • Molybdopterin guanylyltransferase
  • Molybdopterin-guanine dinucleotide biosynthesis protein A
  • Molybdopterin-guanine dinucleotide synthase
  • narB
  • Protein FA
Gene NamemobA
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011207|Molybdenum cofactor guanylyltransferase
MNLMTTITGVVLAGGKARRMGGVDKGLLELNGKPLWQHVADALMTQLSHVVVNANRHQEI
YQASGLKVIEDSLADYPGPLAGMLSVMQQEAGEWFLFCPCDTPYIPPDLAARLNHQRKDA
PVVWVHDGERDHPTIALVNRAIEPLLLEYLQAGERRVMVFMRLAGGHAVDFSDHKDAFVN
VNTPEELARWQEKR
Number of residuesNone
Molecular Weight21642.735
Theoretical pI6.3
GO Classification
Functions
  • GTP binding
  • magnesium ion binding
  • molybdenum cofactor guanylyltransferase activity
Processes
  • bis(molybdopterin guanine dinucleotide)molybdenum biosynthetic process
Components
  • cytoplasm
General FunctionMolybdenum cofactor guanylyltransferase activity
Specific FunctionTransfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. Is also involved in the biosynthesis of the bis-MGD form of the Moco cofactor (Mo-bisMGD) in which the metal is symmetrically ligated by the dithiolene groups of two MGD molecules. Is necessary and sufficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofactor, which implies formation and efficient insertion of the cofactor into the enzyme without the need of a chaperone. Is specific for GTP since other nucleotides such as ATP and GMP can not be utilized.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP32173
UniProtKB Entry Name
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0011208|Molybdenum cofactor guanylyltransferase (mobA)
GTGAATCTGATGACGACGATAACAGGCGTTGTGCTGGCAGGCGGTAAAGCCAGACGAATG
GGCGGCGTAGATAAAGGATTGCTTGAATTAAACGGCAAACCATTATGGCAACATGTCGCT
GACGCGCTTATGACGCAGCTCTCTCACGTCGTGGTTAATGCTAATCGTCATCAGGAAATC
TATCAGGCAAGCGGTCTGAAAGTGATTGAAGATTCACTGGCGGATTACCCAGGCCCTCTG
GCAGGAATGCTTTCAGTAATGCAGCAGGAAGCTGGTGAGTGGTTTTTGTTTTGCCCGTGC
GATACGCCTTACATTCCCCCTGATTTAGCAGCCAGGCTTAATCATCAGCGCAAAGATGCG
CCTGTCGTGTGGGTCCATGACGGTGAACGCGATCACCCGACTATTGCTCTGGTAAACCGC
GCTATTGAGCCTTTATTACTGGAATATCTGCAAGCAGGAGAACGCCGGGTAATGGTATTT
ATGCGTCTGGCTGGCGGTCATGCGGTTGATTTCAGCGATCATAAAGATGCATTTGTTAAC
GTGAATACGCCAGAGGAGCTTGCCCGATGGCAGGAAAAACGATGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Plunkett G 3rd, Burland V, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes. Nucleic Acids Res. 1993 Jul 25;21(15):3391-8. [8346018 ]
  2. 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. [9278503 ]
  3. 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. [16738553 ]
  4. Iobbi-Nivol C, Palmer T, Whitty PW, McNairn E, Boxer DH: The mob locus of Escherichia coli K12 required for molybdenum cofactor biosynthesis is expressed at very low levels. Microbiology. 1995 Jul;141 ( Pt 7):1663-71. [7551035 ]
  5. Palmer T, Vasishta A, Whitty PW, Boxer DH: Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli. Eur J Biochem. 1994 Jun 1;222(2):687-92. [8020507 ]
  6. Johnson JL, Indermaur LW, Rajagopalan KV: Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide. J Biol Chem. 1991 Jul 5;266(19):12140-5. [1648082 ]
  7. Temple CA, Rajagopalan KV: Mechanism of assembly of the Bis(Molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase. J Biol Chem. 2000 Dec 22;275(51):40202-10. [10978348 ]
  8. Magalon A, Frixon C, Pommier J, Giordano G, Blasco F: In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli. J Biol Chem. 2002 Dec 13;277(50):48199-204. Epub 2002 Oct 7. [12372836 ]
  9. Neumann M, Seduk F, Iobbi-Nivol C, Leimkuhler S: Molybdopterin dinucleotide biosynthesis in Escherichia coli: identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides. J Biol Chem. 2011 Jan 14;286(2):1400-8. doi: 10.1074/jbc.M110.155671. Epub 2010 Nov 16. [21081498 ]
  10. Lake MW, Temple CA, Rajagopalan KV, Schindelin H: The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis. J Biol Chem. 2000 Dec 22;275(51):40211-7. [10978347 ]
  11. Stevenson CE, Sargent F, Buchanan G, Palmer T, Lawson DM: Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution. Structure. 2000 Nov 15;8(11):1115-25. [11080634 ]
  12. Guse A, Stevenson CE, Kuper J, Buchanan G, Schwarz G, Giordano G, Magalon A, Mendel RR, Lawson DM, Palmer T: Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobA. J Biol Chem. 2003 Jul 11;278(28):25302-7. Epub 2003 Apr 28. [12719427 ]

From www.t3db.ca