Anaerobic ribonucleoside-triphosphate reductase (P28903)

Identification
Name:Anaerobic ribonucleoside-triphosphate reductase
Synonyms:Not Available
Gene Name:nrdD
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H(2)O = ribonucleoside triphosphate + thioredoxin
Cellular Location:Not Available
SMPDB Pathways:
  • Pyrimidine metabolism PW000942
  • purine nucleotides de novo biosynthesis PW000910
  • purine nucleotides de novo biosynthesis 1435709748 PW000960
  • purine nucleotides de novo biosynthesis 2 PW002033
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thioredoxin disulfide+1.0Thumb ↔ 1.0Thumb+1.0Thioredoxin
1.0dATP + 1.0Thioredoxin disulfide + 1.0Water ↔ 1.0Adenosine triphosphate + 1.0Thioredoxin
ReactionCard
1.0Thumb+1.0Thioredoxin disulfide+1.0Thumb ↔ 1.0Thumb+1.0Thioredoxin
1.0dGTP + 1.0Thioredoxin disulfide + 1.0Water ↔ 1.0Guanosine triphosphate + 1.0Thioredoxin
ReactionCard
1.0Thumb+1.0Thioredoxin disulfide+1.0Thumb ↔ 1.0Thumb+1.0Thioredoxin
1.0dCTP + 1.0Thioredoxin disulfide + 1.0Water ↔ 1.0Cytidine triphosphate + 1.0Thioredoxin
ReactionCard
1.0Thumb+1.0Thioredoxin disulfide+1.0Thumb ↔ 1.0Thumb+1.0Thioredoxin
1.0Deoxyuridine triphosphate + 1.0Thioredoxin disulfide + 1.0Water ↔ 1.0Uridine triphosphate + 1.0Thioredoxin
ReactionCard
1.02'-Deoxyribonucleoside triphosphate+1.0Thioredoxin disulfide+1.0Thumb ↔ 1.0Ribonucleoside triphosphate+1.0Thumb
1.02'-Deoxyribonucleoside triphosphate + 1.0Thioredoxin disulfide + 1.0Water ↔ 1.0Ribonucleoside triphosphate + 1.0Thioredoxin
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0a reduced flavodoxin → 1.0Thumb+1.0an oxidized flavodoxin+1.0Thumb
1.0Guanosine triphosphate + 1.0a reduced flavodoxin → 1.0dGTP + 1.0an oxidized flavodoxin + 1.0Water
ReactionCard
1.0Thumb+1.0a reduced flavodoxin → 1.0an oxidized flavodoxin+1.0Thumb+1.0dATP+1.0Thumb
1.0Adenosine triphosphate + 1.0a reduced flavodoxin → 1.0an oxidized flavodoxin + 1.0Water + 1.0dATP + 1.0dATP
ReactionCard
1.0Thumb+1.0a reduced flavodoxin → 1.0Thumb+1.0an oxidized flavodoxin+1.0Thumb
1.0Cytidine triphosphate + 1.0a reduced flavodoxin → 1.0Water + 1.0an oxidized flavodoxin + 1.0dCTP
ReactionCard
1.0Uridine triphosphate+1.0a reduced flavodoxin+1.0Thumb → 1.0Thumb+1.0an oxidized flavodoxin+1.0Thumb
1.0Uridine triphosphate + 1.0a reduced flavodoxin + 1.0Uridine triphosphate → 1.0Water + 1.0an oxidized flavodoxin + 1.0Deoxyuridine triphosphate
ReactionCard
1.0Thumb+1.0reduced thioredoxin → 1.0oxidized thioredoxin +1.0Thumb+1.0dGDP+1.0Thumb
1.0Guanosine diphosphate + 1.0reduced thioredoxin → 1.0oxidized thioredoxin + 1.0Water + 1.0dGDP + 1.0dGDP
ReactionCard
1.0Adenosine diphosphate+1.0reduced thioredoxin+1.0Thumb ↔ 1.0Thumb+1.0oxidized thioredoxin +1.0dADP+1.0Thumb
1.0Adenosine diphosphate + 1.0reduced thioredoxin + 1.0ADP ↔ 1.0Water + 1.0oxidized thioredoxin + 1.0dADP + 1.0dADP
ReactionCard
1.0Uridine 5'-diphosphate+1.0reduced thioredoxin+1.0Thumb ? 1.0oxidized thioredoxin +1.0Thumb+1.0dUDP+1.0Thumb
1.0Uridine 5'-diphosphate + 1.0reduced thioredoxin + 1.0Uridine 5'-diphosphate ? 1.0oxidized thioredoxin + 1.0Water + 1.0dUDP + 1.0dUDP
ReactionCard
Complex Reactions:
1.0Thumb+2.0Flavodoxin reduced+2.0Thumb → 1.0Thumb+2.0flavodoxin semi oxidized+1.0Thumb
1.0Cytidine triphosphate + 2.0Flavodoxin reduced + 2.0Hydrogen ion → 1.0dCTP + 2.0flavodoxin semi oxidized + 1.0Water
ReactionCard
1.0Thumb+2.0Flavodoxin reduced+2.0Thumb → 1.0Thumb+2.0flavodoxin semi oxidized+1.0Thumb
1.0Adenosine triphosphate + 2.0Flavodoxin reduced + 2.0Hydrogen ion → 1.0dATP + 2.0flavodoxin semi oxidized + 1.0Water
ReactionCard
2.0Flavodoxin reduced+1.0Thumb+2.0Thumb → 1.0Thumb+2.0flavodoxin semi oxidized+1.0Thumb
2.0Flavodoxin reduced + 1.0Guanosine triphosphate + 2.0Hydrogen ion → 1.0dGTP + 2.0flavodoxin semi oxidized + 1.0Water
ReactionCard
2.0Flavodoxin reduced+2.0Thumb+1.0Thumb → 1.0Thumb+2.0flavodoxin semi oxidized+1.0Thumb
2.0Flavodoxin reduced + 2.0Hydrogen ion + 1.0Uridine triphosphate → 1.0Deoxyuridine triphosphate + 2.0flavodoxin semi oxidized + 1.0Water
ReactionCard
1.02'-deoxyribonucleoside triphosphate+1.0thioredoxin disulfide+1.0Thumb → 1.0ribonucleoside triphosphate+1.0thioredoxin
1.02'-deoxyribonucleoside triphosphate + 1.0thioredoxin disulfide + 1.0Water → 1.0ribonucleoside triphosphate + 1.0thioredoxin
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB00082Cytidine triphosphateMetaboCard
ECMDB21326dADPMetaboCard
ECMDB01532dATPMetaboCard
ECMDB00998dCTPMetaboCard
ECMDB01191Deoxyuridine triphosphateMetaboCard
ECMDB00960dGDPMetaboCard
ECMDB01440dGTPMetaboCard
ECMDB01000dUDPMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB01273Guanosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB23749ThioredoxinMetaboCard
ECMDB00295Uridine 5'-diphosphateMetaboCard
ECMDB00285Uridine triphosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on CH or CH2 groups
oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
ribonucleoside-triphosphate reductase activity
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b4238
Gene OrientationCounterclockwise
Centisome Percentage:96.10
Left Sequence End4458545
Right Sequence End4460683
Gene Sequence:
>2139 bp
ATGACACCGCATGTGATGAAACGAGACGGCTGCAAAGTGCCGTTTAAATCAGAGCGCATC
AAAGAAGCGATTCTGCGTGCAGCTAAAGCAGCGGAAGTCGATGATGCCGATTATTGCGCC
ACTGTTGCCGCGGTTGTCAGCGAGCAGATGCAGGGCCGCAACCAGGTGGATATCAATGAG
ATCCAGACCGCAGTTGAAAATCAGCTGATGTCAGGTCCATACAAACAACTGGCTCGTGCT
TACATCGAGTACCGTCACGATCGCGACATTGAACGTGAAAAACGCGGTCGCCTGAACCAG
GAGATCCGTGGTCTGGTCGAGCAGACCAACGCCTCGTTACTCAACGAAAACGCCAACAAA
GACAGCAAGGTGATTCCAACCCAGCGCGACCTGCTGGCCGGGATCGTGGCTAAACACTAT
GCACGTCAGCACCTGCTGCCGCGTGACGTGGTGCAGGCACATGAGCGTGGCGATATTCAC
TATCACGATCTCGATTACTCACCGTTCTTCCCGATGTTCAACTGCATGTTGATCGACCTG
AAAGGCATGCTGACCCAGGGCTTTAAAATGGGGAACGCCGAGATTGAACCGCCGAAGTCG
ATCTCTACGGCAACCGCGGTAACTGCGCAGATTATTGCTCAGGTTGCCAGCCATATTTAT
GGCGGCACCACCATTAACCGTATCGATGAAGTGCTGGCACCGTTTGTCACTGCCAGCTAC
AACAAACATCGCAAGACCGCAGAAGAGTGGAACATCCCGGACGCCGAAGGCTACGCTAAC
TCTCGAACCATCAAAGAGTGCTACGATGCCTTCCAGTCACTGGAGTACGAAGTAAACACC
CTGCACACCGCCAACGGTCAGACGCCGTTTGTAACCTTTGGTTTTGGCCTGGGCACCAGC
TGGGAATCGCGCCTGATTCAGGAATCGATCCTGCGTAACCGTATCGCAGGCCTCGGTAAA
AACCGTAAAACTGCGGTGTTCCCGAAACTGGTGTTTGCGATTCGCGATGGCCTGAACCAT
AAAAAAGGCGATCCGAACTACGACATCAAACAGCTGGCGCTGGAGTGCGCAAGCAAGCGC
ATGTATCCGGATATCCTGAACTACGATCAGGTAGTGAAAGTCACCGGTTCGTTTAAAACT
CCGATGGGCTGCCGCAGCTTCCTCGGCGTGTGGGAAAATGAAAACGGCGAGCAGATCCAC
GATGGTCGTAACAACCTCGGCGTGATCAGCCTGAACCTGCCGCGTATTGCTCTGGAAGCA
AAAGGCGATGAAGCCACCTTCTGGAAGCTGCTGGATGAACGTCTGGTGCTGGCACGTAAG
GCGCTGATGACCCGTATCGCTCGTCTCGAAGGCGTGAAAGCGCGCGTGGCCCCGATCCTC
TATATGGAAGGTGCTTGTGGCGTGCGTCTCAATGCTGACGATGATGTTTCTGAAATCTTC
AAAAACGGTCGTGCGTCTATTTCGCTGGGTTACATCGGCATCCACGAAACCATTAACGCG
CTGTTCGGCGGCGAGCATGTTTACGACAACGAGCAGCTTCGCGCGAAAGGTATCGCCATT
GTTGAACGTCTGCGTCAGGCAGTGGATCAGTGGAAAGAAGAAACGGGTTATGGTTTCAGT
CTCTACAGCACGCCGAGTGAAAACCTGTGCGATCGCTTCTGCCGTCTCGATACTGCTGAG
TTTGGCGTGGTGCCGGGCGTGACCGATAAAGGTTACTACACCAACAGTTTCCACCTCGAT
GTGGAGAAGAAGGTGAACCCGTACGACAAGATCGACTTTGAAGCGCCTTACCCGCCGCTG
GCGAACGGTGGTTTCATTTGCTACGGCGAGTATCCAAACATTCAGCACAACCTGAAGGCG
CTGGAAGATGTCTGGGATTACAGCTATCAGCATGTACCGTATTACGGCACCAATACACCG
ATTGATGAGTGCTACGAGTGTGGCTTTACCGGTGAGTTCGAGTGCACCAGCAAAGGCTTC
ACTTGCCCGAAATGTGGTAACCATGACGCCTCCCGTGTGTCGGTAACTCGCCGCGTGTGC
GGATATTTAGGTAGCCCGGATGCACGTCCGTTTAACGCTGGTAAGCAGGAAGAAGTTAAG
CGCCGCGTTAAACATTTGGGGAATGGGCAGATAGGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:712
Protein Molecular Weight:80022
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Anaerobic ribonucleoside-triphosphate reductase
MTPHVMKRDGCKVPFKSERIKEAILRAAKAAEVDDADYCATVAAVVSEQMQGRNQVDINE
IQTAVENQLMSGPYKQLARAYIEYRHDRDIEREKRGRLNQEIRGLVEQTNASLLNENANK
DSKVIPTQRDLLAGIVAKHYARQHLLPRDVVQAHERGDIHYHDLDYSPFFPMFNCMLIDL
KGMLTQGFKMGNAEIEPPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPFVTASY
NKHRKTAEEWNIPDAEGYANSRTIKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTS
WESRLIQESILRNRIAGLGKNRKTAVFPKLVFAIRDGLNHKKGDPNYDIKQLALECASKR
MYPDILNYDQVVKVTGSFKTPMGCRSFLGVWENENGEQIHDGRNNLGVISLNLPRIALEA
KGDEATFWKLLDERLVLARKALMTRIARLEGVKARVAPILYMEGACGVRLNADDDVSEIF
KNGRASISLGYIGIHETINALFGGEHVYDNEQLRAKGIAIVERLRQAVDQWKEETGYGFS
LYSTPSENLCDRFCRLDTAEFGVVPGVTDKGYYTNSFHLDVEKKVNPYDKIDFEAPYPPL
ANGGFICYGEYPNIQHNLKALEDVWDYSYQHVPYYGTNTPIDECYECGFTGEFECTSKGF
TCPKCGNHDASRVSVTRRVCGYLGSPDARPFNAGKQEEVKRRVKHLGNGQIG
References
External Links:
ResourceLink
Uniprot ID:P28903
Uniprot Name:NRDD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676987
Ecogene ID:EG11417
Ecocyc:EG11417
ColiBase:b4238
Kegg Gene:b4238
EchoBASE ID:EB1388
CCDB:NRDD_ECOLI
BacMap:16132060
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
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • 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
  • Logan, D. T., Mulliez, E., Larsson, K. M., Bodevin, S., Atta, M., Garnaud, P. E., Sjoberg, B. M., Fontecave, M. (2003). "A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase." Proc Natl Acad Sci U S A 100:3826-3831. Pubmed: 12655046
  • Rimmele, M., Boos, W. (1994). "Trehalose-6-phosphate hydrolase of Escherichia coli." J Bacteriol 176:5654-5664. Pubmed: 8083158
  • Sun, X., Eliasson, R., Pontis, E., Andersson, J., Buist, G., Sjoberg, B. M., Reichard, P. (1995). "Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme." J Biol Chem 270:2443-2446. Pubmed: 7852304
  • Sun, X., Harder, J., Krook, M., Jornvall, H., Sjoberg, B. M., Reichard, P. (1993). "A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene." Proc Natl Acad Sci U S A 90:577-581. Pubmed: 8421692