ECMDB

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:

Oxidative phosphorylation PW000919
inner membrane transport PW000786

KEGG Pathways:

Benzoate degradation via CoA ligation ec00632
Butanoate metabolism ec00650
Citrate cycle (TCA cycle) ec00020
Oxidative phosphorylation ec00190
Reductive carboxylate cycle (CO2 fixation) ec00720

KEGG Reactions:

1.0

↔

1.0

1.0Succinic acid + 1.0FAD ↔ 1.0FADH2 + 1.0Fumaric acid
ReactionCard

1.0

1.0Acceptor

↔

1.0

1.0Reduced acceptor

1.0Succinic acid + 1.0Acceptor ↔ 1.0Fumaric acid + 1.0Reduced acceptor
ReactionCard

1.0

↔

1.0

1.0Succinic acid + 1.0Quinone ↔ 1.0Fumaric acid + 1.0Hydroquinone
ReactionCard

SMPDB Reactions:

1.0

2.0

1.0a menaquinol

→

1.0

1.0a menaquinone

1.0Fumaric acid + 2.0Hydrogen ion + 1.0a menaquinol → 1.0Succinic acid + 1.0a menaquinone
ReactionCard

Complex Reactions:

1.0

→

1.0Menaquinone 8

1.0

1.0Fumaric acid + 1.0Menaquinol 8 → 1.0Menaquinone 8 + 1.0Succinic acid
ReactionCard

1.0

→

1.0

1.02-Demethylmenaquinol 8 + 1.0Fumaric acid → 1.02-Demethylmenaquinone 8 + 1.0Succinic acid
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB21154	2-Demethylmenaquinol 8	MetaboCard
ECMDB21155	2-Demethylmenaquinone 8	MetaboCard
ECMDB01248	FAD	MetaboCard
ECMDB01197	FADH2	MetaboCard
ECMDB00176	Fumaric acid	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB02434	Hydroquinone	MetaboCard
ECMDB21245	Menaquinol 8	MetaboCard
ECMDB23060	Quinone	MetaboCard
ECMDB00254	Succinic acid	MetaboCard

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 Orientation

Counterclockwise

Centisome Percentage:

94.37

Left Sequence End

4378533

Right Sequence End

4380341

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:

FAD_binding_2 (PF00890 )
Succ_DH_flav_C (PF02910 )

Protein Residues:

602

Protein Molecular Weight:

65971

Protein Theoretical pI:

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:

Resource	Link
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

Fumarate reductase flavoprotein subunit (P00363)