RegulonDB RegulonDB 11.1: Gene Form
   

moaA gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

moaA ybhK moaB CueR ModE FNR Cis-reg; riboswitch TSS_948 (cluster) TSS_948 (cluster) moaBp moaBp moaAp2 moaAp2 TSS_945 (cluster) TSS_945 (cluster) TSS_944 TSS_944 moaAp1 moaAp1 ybhKp ybhKp TSS_942 (cluster) TSS_942 (cluster)

Gene      
Name: moaA    Texpresso search in the literature
Synonym(s): ECK0770, EG11595, b0781, bisA, chlA, chlA1, narA
Genome position(nucleotides): 817044 --> 818033
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 54.14
External database links:  
ASAP:
 ABE-0002669
CGSC:
 922
ECHOBASE:
 EB1552
ECOLIHUB:
 moaA
MIM:
 252150
OU-MICROARRAY:
 b0781
STRING:
 511145.b0781
COLOMBOS: moaA


Product      
Name: GTP 3',8'-cyclase
Synonym(s): BisA, ChlA, MoaA, NarA, molybdopterin biosynthesis protein A
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 37.346
Isoelectric point: 8.083
Motif(s):
 
Type Positions Sequence Comment
8 -> 234 AFARKFYYLRLSITDVCNFRCTYCLPDGYKPSGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFTDIIAAVRENDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVKVNTVLMRDVNHHQLDTFLNWIQHRPIQLRFIELMETGEGSELFRKHHISGQVLRDELLRRGWIHQLRQRSDGPA UniProt: Radical SAM core.
19 -> 181 SITDVCNFRCTYCLPDGYKPSGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFTDIIAAVRENDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVKVNTVLMRDVNHHQLDTFLNWI
23 -> 125 VCNFRCTYCLPDGYKPSGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFTDIIAAVRENDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVD
186 -> 312 IQLRFIELMETGEGSELFRKHHISGQVLRDELLRRGWIHQLRQRSDGPAQVFCHPDYAGEIGLIMPYEKDFCATCNRLRVSSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTHF
262 -> 264 RLR UniProt: GTP.

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.3 - cofactors, small molecule carriers --> 1.5.3.4 - molybdenum
Gene Ontology Terms (GO)  
cellular_component GO:0005829 - cytosol
GO:0019008 - molybdopterin synthase complex
molecular_function GO:0003824 - catalytic activity
GO:0016829 - lyase activity
GO:0046872 - metal ion binding
GO:0000166 - nucleotide binding
GO:0005525 - GTP binding
GO:0051536 - iron-sulfur cluster binding
GO:0051539 - 4 iron, 4 sulfur cluster binding
GO:1904047 - S-adenosyl-L-methionine binding
GO:0061798 - GTP 3',8'-cyclase activity
GO:0061799 - cyclic pyranopterin monophosphate synthase activity
biological_process GO:0006777 - Mo-molybdopterin cofactor biosynthetic process
GO:0009408 - response to heat
Note(s): Note(s): ...[more].
Reference(s): [1] Adhya S., et al., 1968
[2] Amy NK. 1981
[3] Baker KP., et al., 1991
[4] Bilous PT., et al., 1985
[5] Buhning M., et al., 2017
[6] Campbell AM., et al., 1985
[7] Clark DP. 1990
[8] Dykhuizen D. 1973
[9] Giordano G., et al., 1980
[10] Giordano G., et al., 1987
[11] Giordano G., et al., 1985
[12] Giordano G., et al., 1984
[13] Grillet L., et al., 1983
[14] Hackett CS., et al., 1981
[15] Kurata T., et al., 2013
[16] Lambdren PR., et al., 1976
[17] MacGregor CH., et al., 1973
[18] MacGregor CH., et al., 1971
[19] Mutaftschiev S., et al., 1976
[20] Pang H., et al., 2018
[21] Pascal MC., et al., 1982
[22] Pitterle DM., et al., 1989
[23] Reiss J., et al., 1987
[24] Saracino L., et al., 1986
[25] Skotnicki ML., et al., 1979
[26] Takagi M., et al., 1981
[27] Taylor JL., et al., 1983
[28] del Campillo-Campbell A., et al., 1982
External database links:  
ALPHAFOLD:
 P30745
DIP:
 DIP-10228N
ECOCYC:
 EG11595-MONOMER
ECOLIWIKI:
 b0781
INTERPRO:
 IPR013483
INTERPRO:
 IPR013785
INTERPRO:
 IPR010505
INTERPRO:
 IPR007197
INTERPRO:
 IPR006638
INTERPRO:
 IPR000385
MODBASE:
 P30745
PFAM:
 PF06463
PFAM:
 PF04055
PFAM:
 PF13353
PRIDE:
 P30745
PRODB:
 PRO_000023260
PROSITE:
 PS01305
PROSITE:
 PS51918
REFSEQ:
 NP_415302
SMART:
 SM00729
SMR:
 P30745
UNIPROT:
 P30745


Operon      
Name: moaABCDE         
Operon arrangement:
Transcription unit        Promoter
moaABCDE
moaABCDE
moaBCDE


Transcriptional Regulation      
Display Regulation             
Activated by: FNR, ModE
Repressed by: CueR


RNA cis-regulatory element    
   
Cis-reg; riboswitch Moco (molybdenum cofactor) riboswitch
   
   


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_942 (cluster) 816671 reverse nd [RS-EPT-CBR] [29]
  promoter ybhKp 816692 reverse We assigned a putative transcription
Read more > 		[COMP-AINF], [COMP-AINF-POSITIONAL-IDENTIFICATION], [COMP-AINF-SIMILAR-TO-CONSENSUS] [30], [31]
  promoter TSS_944 816830 forward nd [RS-EPT-CBR] [29]
  promoter TSS_945 (cluster) 816858 forward nd [RS-EPT-CBR] [29]
  promoter TSS_948 (cluster) 818012 forward nd [RS-EPT-CBR] [29]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

 [COMP-AINF] Inferred computationally without human oversight

 [COMP-AINF-POSITIONAL-IDENTIFICATION] Automated inference of promoter position

 [COMP-AINF-SIMILAR-TO-CONSENSUS] Automated inference based on similarity to consensus sequences


Reference(s)    

 [1] Adhya S., Cleary P., Campbell A., 1968, A deletion analysis of prophage lambda and adjacent genetic regions., Proc Natl Acad Sci U S A 61(3):956-62

 [2] Amy NK., 1981, Identification of the molybdenum cofactor in chlorate-resistant mutants of Escherichia coli., J Bacteriol 148(1):274-82

 [3] Baker KP., Boxer DH., 1991, Regulation of the chlA locus of Escherichia coli K12: involvement of molybdenum cofactor., Mol Microbiol 5(4):901-7

 [4] Bilous PT., Weiner JH., 1985, Dimethyl sulfoxide reductase activity by anaerobically grown Escherichia coli HB101., J Bacteriol 162(3):1151-5

 [5] Buhning M., Valleriani A., Leimkuhler S., 2017, The Role of SufS Is Restricted to Fe-S Cluster Biosynthesis in Escherichia coli., Biochemistry 56(14):1987-2000

 [6] Campbell AM., del Campillo-Campbell A., Villaret DB., 1985, Molybdate reduction by Escherichia coli K-12 and its chl mutants., Proc Natl Acad Sci U S A 82(1):227-31

 [7] Clark DP., 1990, Molybdenum cofactor negative mutants of Escherichia coli use citrate anaerobically., FEMS Microbiol Lett 55(3):245-9

 [8] Dykhuizen D., 1973, Genetic analysis of the system that reduces biotin-d-sulfoxide in Escherichia coli., J Bacteriol 115(2):662-7

 [9] Giordano G., Grillet L., Pommier J., Terriere C., Haddock BA., Azoulay E., 1980, Precursor forms of the subunits of nitrate reductase in chlA and chlB mutants of Escherichia coli K12., Eur J Biochem 105(2):297-306

 [10] Giordano G., Santini CL., Saracino L., Iobbi C., 1987, Involvement of a protein with molybdenum cofactor in the in vitro activation of nitrate reductase from a chlA mutant of Escherichia coli K12., Biochim Biophys Acta 914(3):220-32

 [11] Giordano G., Saracino L., Grillet L., 1985, Identification in various chlorate-resistant mutants of a protein involved in the activation of nitrate reductase in the soluble fraction of a chlA mutant of Escherichia coli K-12., Biochim Biophys Acta 839(2):181-90

 [12] Giordano G., Violet M., Medani CL., Pommier J., 1984, A common pathway for the activation of several molybdoenzymes in Escherichia coli K12., Biochim Biophys Acta 798(2):216-25

 [13] Grillet L., Giordano G., 1983, Identification and purification of a protein involved in the activation of nitrate reductase in the soluble fraction of a chlA mutant of Escherichia coli K12., Biochim Biophys Acta 749(1):115-24

 [14] Hackett CS., MacGregor CH., 1981, Synthesis and degradation of nitrate reductase in Escherichia coli., J Bacteriol 146(1):352-9

 [15] Kurata T., Katayama A., Hiramatsu M., Kiguchi Y., Takeuchi M., Watanabe T., Ogasawara H., Ishihama A., Yamamoto K., 2013, Identification of the set of genes, including nonannotated morA, under the direct control of ModE in Escherichia coli., J Bacteriol 195(19):4496-505

 [16] Lambdren PR., Guest JR., 1976, A novel method for isolating chlorate-resistant mutants of Escherichia coli K12 by anaerobic selection on a lactate plus fumarate medium., J Gen Microbiol 93(1):173-6

 [17] MacGregor CH., Schnaitman CA., 1973, Reconstitution of nitrate reductase activity and formation of membrane particles from cytoplasmic extracts of chlorate-resistant mutants of Escherichia coli., J Bacteriol 114(3):1164-76

 [18] MacGregor CH., Schnaitman CA., 1971, Alterations in the cytoplasmic membrane proteins of various chlorate-resistant mutants of Escherichia coli., J Bacteriol 108(1):564-70

 [19] Mutaftschiev S., Olive J., Azoulay E., 1976, [Ultrastructure of the particles reconstituted by complementation of extracts from chl-r mutants of Escherichia coli K 12]., C R Acad Sci Hebd Seances Acad Sci D 283(7):825-8

 [20] Pang H., Yokoyama K., 2018, Lessons From the Studies of a CC Bond Forming Radical SAM Enzyme in Molybdenum Cofactor Biosynthesis., Methods Enzymol 606:485-522

 [21] Pascal MC., Burini JF., Ratouchniak J., Chippaux M., 1982, Regulation of the nitrate reductase operon: effect of mutations in chlA, B, D and E genes., Mol Gen Genet 188(1):103-6

 [22] Pitterle DM., Rajagopalan KV., 1989, Two proteins encoded at the chlA locus constitute the converting factor of Escherichia coli chlA1., J Bacteriol 171(6):3373-8

 [23] Reiss J., Kleinhofs A., Klingmuller W., 1987, Cloning of seven differently complementing DNA fragments with chl functions from Escherichia coli K12., Mol Gen Genet 206(2):352-5

 [24] Saracino L., Violet M., Boxer DH., Giordano G., 1986, Activation in vitro of respiratory nitrate reductase of Escherichia coli K12 grown in the presence of tungstate. Involvement of molybdenum cofactor., Eur J Biochem 158(3):483-90

 [25] Skotnicki ML., Rolfe BG., 1979, Pathways of energy metabolism required for phenotypic expression of nif+Kp genes in Escherichia coli., Aust J Biol Sci 32(6):637-49

 [26] Takagi M., Tsuchiya T., Ishimoto M., 1981, Proton translocation coupled to trimethylamine N-oxide reduction in anaerobically grown Escherichia coli., J Bacteriol 148(3):762-8

 [27] Taylor JL., Bedbrook JR., Grant FJ., Kleinhofs A., 1983, Reconstitution of plant nitrate reductase by Escherichia coli extracts and the molecular cloning of the chlA gene of Escherichia coli K12., J Mol Appl Genet 2(3):261-71

 [28] del Campillo-Campbell A., Campbell A., 1982, Molybdenum cofactor requirement for biotin sulfoxide reduction in Escherichia coli., J Bacteriol 149(2):469-78

 [29] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

 [30] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

 [31] Reitzer L., Schneider BL., 2001, Metabolic context and possible physiological themes of sigma(54)-dependent genes in Escherichia coli., Microbiol Mol Biol Rev 65(3):422-44, table of contents

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