Fumarate reductase iron-sulfur subunit (P0AC47)

Identification
Name:Fumarate reductase iron-sulfur subunit
Synonyms:Not Available
Gene Name:frdB
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:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Succinic acid + 1.0FAD ↔ 1.0FADH2 + 1.0Fumaric acid
ReactionCard
1.0Thumb+1.0Acceptor ↔ 1.0Thumb+1.0Reduced acceptor
1.0Succinic acid + 1.0Acceptor ↔ 1.0Fumaric acid + 1.0Reduced acceptor
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Succinic acid + 1.0Quinone ↔ 1.0Fumaric acid + 1.0Hydroquinone
ReactionCard
SMPDB Reactions:
1.0Thumb+2.0Thumb+1.0a menaquinol → 1.0Thumb+1.0a menaquinone
1.0Fumaric acid + 2.0Hydrogen ion + 1.0a menaquinol → 1.0Succinic acid + 1.0a menaquinone
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Menaquinone 8+1.0Thumb
1.0Fumaric acid + 1.0Menaquinol 8 → 1.0Menaquinone 8 + 1.0Succinic acid
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Demethylmenaquinol 8 + 1.0Fumaric acid → 1.02-Demethylmenaquinone 8 + 1.0Succinic acid
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
binding
catalytic activity
electron carrier activity
iron-sulfur cluster binding
metal cluster binding
oxidoreductase activity
Process
acetyl-CoA catabolic process
acetyl-CoA metabolic process
cellular metabolic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
oxidation reduction
tricarboxylic acid cycle
Gene Properties
Blattner:b4153
Gene OrientationCounterclockwise
Centisome Percentage:94.36
Left Sequence End4377806
Right Sequence End4378540
Gene Sequence:
>735 bp
ATGAAAATTGACCTGAACGCCGATCTGGGCGAAGGCTGCGCCAGCGACGCAGAGCTATTA
ACGCTGGTTTCCTCTGCCAATATTGCCTGTGGATTTCATGCAGGCGATGCGCAAATCATG
CAGGCTTGCGTGCGTGAAGCAATAAAAAATGGTGTCGCGATTGGCGCTCACCCGAGTTTT
CCCGACAGGGAAAATTTTGGTCGCAGCGCCATGCAGCTGCCGCCAGAAACCGTTTACGCC
CAGACGCTGTATCAAATTGGCGCGCTGGCAACGATTGCCCGTGCGCAAGGCGGCGTAATG
CGTCATGTCAAACCGCACGGCATGTTGTACAACCAGGCGGCGAAAGAAGCACAACTGGCA
GACGCCATCGCCAGAGCGGTATACGCTTGCGATCCAGCATTGATTCTCGTCGGGCTGGCG
GGAAGCGAGCTGATTCGTGCAGGCAAGCAATATGGTCTGACAACGCGCGAGGAAGTGTTT
GCCGATCGCGGTTATCAGGCTGACGGCTCGCTGGTGCCGCGAAGCCAGTCAGGCGCGTTG
ATTGAAAACGAAGAACAGGCGCTGGCGCAAACGCTGGAGATGGTGCAACACGGCAGAGTC
AAAAGTATCACCGGCGAATGGGCAACGGTCGCGGCGCAAACGGTCTGCCTGCATGGCGAC
GGCGAGCACGCACTGGCGTTCGCCCGCCGACTACGCTCTGCATTTGCCGAAAAGGGGATT
GTTGTCGCAGCATAA
Protein Properties
Pfam Domain Function:Not Available
Protein Residues:244
Protein Molecular Weight:27123
Protein Theoretical pI:6
PDB File:1L0V
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Fumarate reductase iron-sulfur subunit
MAEMKNLKIEVVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRM
AICGSCGMMVNNVPKLACKTFLRDYTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPY
IIGNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPEFIGPAAITLAHRY
NEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESSKDFLIAT
LKPR
References
External Links:
ResourceLink
Uniprot ID:P0AC47
Uniprot Name:FRDB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062309
PDB ID:1L0V
Ecogene ID:EG10331
Ecocyc:EG10331
ColiBase:b4153
Kegg Gene:b4153
EchoBASE ID:EB0327
CCDB:FRDB_ECOLI
BacMap:16131978
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
  • Cole, S. T., Grundstrom, T., Jaurin, B., Robinson, J. J., Weiner, J. H. (1982). "Location and nucleotide sequence of frdB, the gene coding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli." Eur J Biochem 126:211-216. Pubmed: 6751816
  • Grundstrom, T., Jaurin, B. (1982). "Overlap between ampC and frd operons on the Escherichia coli chromosome." Proc Natl Acad Sci U S A 79:1111-1115. Pubmed: 7041115
  • 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
  • Werth, M. T., Cecchini, G., Manodori, A., Ackrell, B. A., Schroder, I., Gunsalus, R. P., Johnson, M. K. (1990). "Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster." Proc Natl Acad Sci U S A 87:8965-8969. Pubmed: 2174169