Flavodoxin-1 (P61949)

Identification
Name:Flavodoxin-1
Synonyms:Not Available
Gene Name:fldA
Enzyme Class:Not Available
Biological Properties
General Function:Involved in FMN binding
Specific Function:Low-potential electron donor to a number of redox enzymes (Potential). Involved in the reactivation of inactive cob(II)alamin in methionine synthase
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+6.0Reduced flavodoxin+1.0Thumb ↔ 1.0Thumb+1.0Thumb+6.0Oxidized flavodoxin+2.0Thumb
1.0Adenosine triphosphate + 1.0Nitrogen + 6.0Reduced flavodoxin + 1.0Water ↔ 1.0Phosphate + 1.0ADP + 6.0Oxidized flavodoxin + 2.0Ammonia
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+6.0a reduced flavodoxin+1.0Thumb ↔ 1.0Thumb+1.0Adenosine diphosphate+1.0an oxidized flavodoxin+2.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Nitrogen + 6.0a reduced flavodoxin + 1.0Water ↔ 1.0Phosphate + 1.0Adenosine diphosphate + 1.0an oxidized flavodoxin + 2.0Ammonia + 1.0ADP
ReactionCard
Complex Reactions:
1.0Thumb+2.0flavodoxin semi oxidized+1.0Thumb ↔ 1.0Thumb+1.0Thumb+2.0Flavodoxin reduced+1.0Thumb
1.0Coenzyme A + 2.0flavodoxin semi oxidized + 1.0Pyruvic acid ↔ 1.0Acetyl-CoA + 1.0Carbon dioxide + 2.0Flavodoxin reduced + 1.0Hydrogen ion
ReactionCard
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
2.0flavodoxin semi oxidized+1.0Thumb → 2.0Flavodoxin reduced+1.0Thumb+1.0Thumb
2.0flavodoxin semi oxidized + 1.0NADPH → 2.0Flavodoxin reduced + 1.0Hydrogen ion + 1.0NADP
ReactionCard
1.0Thumb+2.0Flavodoxin reduced+1.0Thumb → 2.0flavodoxin semi oxidized+1.0Thumb+1.0Thumb
1.02-C-Methyl-D-erythritol-2,4-cyclodiphosphate + 2.0Flavodoxin reduced + 1.0Hydrogen ion → 2.0flavodoxin semi oxidized + 1.01-Hydroxy-2-methyl-2-butenyl 4-diphosphate + 1.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB200201-Hydroxy-2-methyl-2-butenyl 4-diphosphateMetaboCard
ECMDB041032-C-Methyl-D-erythritol-2,4-cyclodiphosphateMetaboCard
ECMDB01206Acetyl-CoAMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB00082Cytidine triphosphateMetaboCard
ECMDB01532dATPMetaboCard
ECMDB00998dCTPMetaboCard
ECMDB01191Deoxyuridine triphosphateMetaboCard
ECMDB01440dGTPMetaboCard
ECMDB01273Guanosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB04114NitrogenMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB00285Uridine triphosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
electron carrier activity
FMN binding
nucleotide binding
oxidoreductase activity
Gene Properties
Blattner:b0684
Gene OrientationCounterclockwise
Centisome Percentage:15.31
Left Sequence End710158
Right Sequence End710688
Gene Sequence:
>531 bp
ATGATTCTTATAATTTATGCGCATCCGTATCCGCATCATTCCCATGCGAATAAACGGATG
CTTGAACAGGCAAGGACGCTGGAAGGCGTCGAAATTCGCTCTCTTTATCAACTCTATCCT
GACTTCAATATCGATATTGCCGCCGAGCAGGAGGCGCTGTCTCGCGCCGATCTGATCGTC
TGGCAGCATCCGATGCAGTGGTACAGCATTCCTCCGCTCCTCAAACTTTGGATCGATAAA
GTTTTCTCCCACGGCTGGGCTTACGGTCATGGCGGCACGGCGCTGCATGGCAAACATTTG
CTGTGGGCGGTGACGACCGGCGGCGGGGAAAGCCATTTTGAAATTGGTGCGCATCCGGGC
TTTGATGTGCTGTCGCAGCCGCTACAGGCGACGGCAATCTACTGCGGGCTGAACTGGCTG
CCACCGTTTGCCATGCACTGCACCTTTATTTGTGACGACGAAACCCTCGAAGGGCAGGCG
CGTCACTATAAGCAACGTCTGCTGGAATGGCAGGAGGCCCATCATGGATAG
Protein Properties
Pfam Domain Function:
Protein Residues:176
Protein Molecular Weight:19737
Protein Theoretical pI:4
PDB File:1AHN
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Flavodoxin-1
MAITGIFFGSDTGNTENIAKMIQKQLGKDVADVHDIAKSSKEDLEAYDILLLGIPTWYYG
EAQCDWDDFFPTLEEIDFNGKLVALFGCGDQEDYAEYFCDALGTIRDIIEPRGATIVGHW
PTAGYHFEASKGLADDDHFVGLAIDEDRQPELTAERVEKWVKQISEELHLDEILNA
References
External Links:
ResourceLink
Uniprot ID:P61949
Uniprot Name:FLAV_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674301
PDB ID:1AHN
Ecogene ID:EG10318
Ecocyc:EG10318
ColiBase:b0684
Kegg Gene:b0684
EchoBASE ID:EB0314
CCDB:FLAV_ECOLI
BacMap:16128660
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
  • Hoover, D. M., Ludwig, M. L. (1997). "A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution." Protein Sci 6:2525-2537. Pubmed: 9416602
  • Jarrett, J. T., Hoover, D. M., Ludwig, M. L., Matthews, R. G. (1998). "The mechanism of adenosylmethionine-dependent activation of methionine synthase: a rapid kinetic analysis of intermediates in reductive methylation of Cob(II)alamin enzyme." Biochemistry 37:12649-12658. Pubmed: 9730838
  • Jenkins, C. M., Waterman, M. R. (1994). "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities." J Biol Chem 269:27401-27408. Pubmed: 7961651
  • Osborne, C., Chen, L. M., Matthews, R. G. (1991). "Isolation, cloning, mapping, and nucleotide sequencing of the gene encoding flavodoxin in Escherichia coli." J Bacteriol 173:1729-1737. Pubmed: 1999390
  • 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
  • Ponstingl, H., Otting, G. (1997). "NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin." Eur J Biochem 244:384-399. Pubmed: 9119004