Identification
Name:Fumarate reductase flavoprotein subunit
Synonyms:Not Available
Gene Name:frdA
Enzyme Class:
Biological Properties
General Function:Involved in electron carrier activity
Specific Function:Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+AcceptorThumb+Reduced acceptor
Succinic acid + Acceptor ↔ Fumaric acid + Reduced acceptor
ReactionCard
Thumb+ThumbThumb+Thumb
SMPDB Reactions:
Thumb+2 Thumb+"a menaquinol"Thumb+"a menaquinone"
Fumaric acid + 2 Hydrogen ion + "a menaquinol" → Succinic acid + "a menaquinone"
ReactionCard
Complex Reactions:
Thumb+ThumbMenaquinone 8+Thumb
Thumb+ThumbThumb+Thumb
Thumb+acceptorThumb+reduced acceptor
Succinic acid + acceptor → Fumaric acid + reduced acceptor
ReactionCard
Thumb+acceptorThumb+reduced acceptor
Succinic acid + acceptor → Fumaric acid + reduced acceptor
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211542-Demethylmenaquinol 8MetaboCard
ECMDB211552-Demethylmenaquinone 8MetaboCard
ECMDB01248FADMetaboCard
ECMDB01197FADH2MetaboCard
ECMDB00176Fumaric acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB02434HydroquinoneMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB23060QuinoneMetaboCard
ECMDB00254Succinic acidMetaboCard
GO Classification:
Function
adenyl nucleotide binding
binding
catalytic activity
electron carrier activity
FAD or FADH2 binding
nucleoside binding
oxidoreductase activity
oxidoreductase activity, acting on the CH-CH group of donors
purine nucleoside binding
Process
anaerobic respiration
cellular metabolic process
cellular respiration
electron transport chain
energy derivation by oxidation of organic compounds
generation of precursor metabolites and energy
metabolic process
oxidation reduction
Gene Properties
Blattner:b4154
Gene OrientationCounterclockwise
Centisome Percentage:94.37
Left Sequence End4378533
Right Sequence End4380341
Gene Sequence:
>1809 bp
GTGCAAACCTTTCAAGCCGATCTTGCCATTGTAGGCGCCGGTGGCGCGGGATTACGTGCT
GCAATTGCTGCCGCGCAGGCAAATCCGAATGCAAAAATCGCACTAATCTCAAAAGTATAC
CCGATGCGTAGCCATACCGTTGCTGCAGAAGGGGGCTCCGCCGCTGTCGCGCAGGATCAT
GACAGCTTCGAATATCACTTTCACGATACAGTAGCGGGTGGCGACTGGTTGTGTGAGCAG
GATGTCGTGGATTATTTCGTCCACCACTGCCCAACCGAAATGACCCAACTGGAACTGTGG
GGATGCCCATGGAGCCGTCGCCCGGATGGTAGCGTCAACGTACGTCGCTTCGGCGGCATG
AAAATCGAGCGCACCTGGTTCGCCGCCGATAAGACCGGCTTCCATATGCTGCACACGCTG
TTCCAGACCTCTCTGCAATTCCCGCAGATCCAGCGTTTTGACGAACATTTCGTGCTGGAT
ATTCTGGTTGATGATGGTCATGTTCGCGGCCTGGTAGCAATGAACATGATGGAAGGCACG
CTGGTGCAGATCCGTGCTAACGCGGTCGTTATGGCTACTGGCGGTGCGGGTCGCGTTTAT
CGTTACAACACCAACGGCGGCATCGTTACCGGTGACGGTATGGGTATGGCGCTAAGCCAC
GGCGTTCCGCTGCGTGACATGGAATTCGTTCAGTATCACCCAACCGGTCTGCCAGGTTCC
GGTATCCTGATGACCGAAGGTTGCCGCGGTGAAGGCGGTATTCTGGTCAACAAAAATGGC
TACCGTTATCTGCAAGATTACGGCATGGGCCCGGAAACTCCGCTGGGCGAGCCGAAAAAC
AAATATATGGAACTGGGTCCACGCGACAAAGTCTCTCAGGCCTTCTGGCACGAATGGCGT
AAAGGCAACACCATCTCCACGCCGCGTGGCGATGTGGTTTATCTCGACTTGCGTCACCTC
GGCGAGAAAAAACTGCATGAACGTCTGCCGTTCATCTGCGAACTGGCGAAAGCGTACGTT
GGCGTCGATCCGGTTAAAGAACCGATTCCGGTACGTCCGACCGCACACTACACCATGGGC
GGTATCGAAACCGATCAGAACTGTGAAACCCGCATTAAAGGTCTGTTCGCCGTGGGTGAA
TGTTCCTCTGTTGGTCTGCACGGTGCAAACCGTCTGGGTTCTAACTCCCTGGCGGAACTG
GTGGTCTTCGGCCGTCTGGCCGGTGAACAAGCGACAGAGCGTGCAGCAACTGCCGGTAAT
GGCAACGAAGCGGCAATTGAAGCGCAGGCAGCTGGCGTTGAACAACGTCTGAAAGATCTG
GTTAACCAGGATGGCGGCGAAAACTGGGCGAAGATCCGCGACGAAATGGGCCTGGCTATG
GAAGAAGGCTGCGGTATCTACCGTACGCCGGAACTGATGCAGAAAACCATCGACAAGCTG
GCAGAGCTGCAGGAACGCTTCAAGCGCGTGCGCATCACCGACACTTCCAGCGTGTTCAAC
ACCGACCTGCTCTACACCATTGAACTGGGCCACGGTCTGAACGTTGCTGAATGTATGGCG
CACTCCGCAATGGCACGTAAAGAGTCCCGCGGCGCGCACCAGCGTCTGGACGAAGGTTGC
ACCGAGCGTGACGACGTCAACTTCCTCAAACACACCCTCGCCTTCCGCGATGCTGATGGC
ACGACTCGCCTGGAGTACAGCGACGTGAAGATTACTACGCTGCCGCCAGCTAAACGCGTT
TACGGTGGCGAAGCGGATGCAGCCGATAAGGCGGAAGCAGCCAATAAGAAGGAGAAGGCG
AATGGCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:602
Protein Molecular Weight:65971
Protein Theoretical pI:6
PDB File:1L0V
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Fumarate reductase flavoprotein subunit
MQTFQADLAIVGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAEGGSAAVAQDH
DSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLELWGCPWSRRPDGSVNVRRFGGM
KIERTWFAADKTGFHMLHTLFQTSLQFPQIQRFDEHFVLDILVDDGHVRGLVAMNMMEGT
LVQIRANAVVMATGGAGRVYRYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPTGLPGS
GILMTEGCRGEGGILVNKNGYRYLQDYGMGPETPLGEPKNKYMELGPRDKVSQAFWHEWR
KGNTISTPRGDVVYLDLRHLGEKKLHERLPFICELAKAYVGVDPVKEPIPVRPTAHYTMG
GIETDQNCETRIKGLFAVGECSSVGLHGANRLGSNSLAELVVFGRLAGEQATERAATAGN
GNEAAIEAQAAGVEQRLKDLVNQDGGENWAKIRDEMGLAMEEGCGIYRTPELMQKTIDKL
AELQERFKRVRITDTSSVFNTDLLYTIELGHGLNVAECMAHSAMARKESRGAHQRLDEGC
TERDDVNFLKHTLAFRDADGTTRLEYSDVKITTLPPAKRVYGGEADAADKAEAANKKEKA
NG
References
External Links:
ResourceLink
Uniprot ID:P00363
Uniprot Name:FRDA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676908
PDB ID:1L0V
Ecogene ID:EG10330
Ecocyc:EG10330
ColiBase:b4154
Kegg Gene:b4154
EchoBASE ID:EB0326
CCDB:FRDA_ECOLI
BacMap:16131979
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
  • Blaut, M., Whittaker, K., Valdovinos, A., Ackrell, B. A., Gunsalus, R. P., Cecchini, G. (1989). "Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin." J Biol Chem 264:13599-13604. Pubmed: 2668268
  • 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
  • Cole, S. T. (1982). "Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli." Eur J Biochem 122:479-484. Pubmed: 7037404
  • 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
  • Iverson, T. M., Luna-Chavez, C., Cecchini, G., Rees, D. C. (1999). "Structure of the Escherichia coli fumarate reductase respiratory complex." Science 284:1961-1966. Pubmed: 10373108
  • Iverson, T. M., Luna-Chavez, C., Croal, L. R., Cecchini, G., Rees, D. C. (2002). "Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site." J Biol Chem 277:16124-16130. Pubmed: 11850430
  • Schroder, I., Gunsalus, R. P., Ackrell, B. A., Cochran, B., Cecchini, G. (1991). "Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis." J Biol Chem 266:13572-13579. Pubmed: 1856194
  • Yi, X., Mroczko, M., Manoj, K. M., Wang, X., Hager, L. P. (1999). "Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue." Proc Natl Acad Sci U S A 96:12412-12417. Pubmed: 10535936