Fumarate reductase flavoprotein subunit

Details

Name
Fumarate reductase flavoprotein subunit
Synonyms
  • 1.3.5.4
Gene Name
frdA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0010381|Fumarate reductase flavoprotein subunit
MQTFQADLAIVGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAEGGSAAVAQDH
DSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLELWGCPWSRRPDGSVNVRRFGGM
KIERTWFAADKTGFHMLHTLFQTSLQFPQIQRFDEHFVLDILVDDGHVRGLVAMNMMEGT
LVQIRANAVVMATGGAGRVYRYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPTGLPGS
GILMTEGCRGEGGILVNKNGYRYLQDYGMGPETPLGEPKNKYMELGPRDKVSQAFWHEWR
KGNTISTPRGDVVYLDLRHLGEKKLHERLPFICELAKAYVGVDPVKEPIPVRPTAHYTMG
GIETDQNCETRIKGLFAVGECSSVGLHGANRLGSNSLAELVVFGRLAGEQATERAATAGN
GNEAAIEAQAAGVEQRLKDLVNQDGGENWAKIRDEMGLAMEEGCGIYRTPELMQKTIDKL
AELQERFKRVRITDTSSVFNTDLLYTIELGHGLNVAECMAHSAMARKESRGAHQRLDEGC
TERDDVNFLKHTLAFRDADGTTRLEYSDVKITTLPPAKRVYGGEADAADKAEAANKKEKA
NG
Number of residues
602
Molecular Weight
65971.215
Theoretical pI
6.24
GO Classification
Functions
electron carrier activity / FAD binding / succinate dehydrogenase activity
Processes
anaerobic respiration / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / cellular response to DNA damage stimulus / electron transport chain / fermentation
Components
cytosol / membrane / plasma membrane fumarate reductase complex
General Function
Succinate dehydrogenase 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0010382|Fumarate reductase flavoprotein subunit (frdA)
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
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00363
UniProtKB Entry NameFRDA_ECOLI
GenBank Protein ID145263
GenBank Gene IDJ01611
General References
  1. Cole ST: Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli. Eur J Biochem. 1982 Mar 1;122(3):479-84. [Article]
  2. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Blaut M, Whittaker K, Valdovinos A, Ackrell BA, Gunsalus RP, Cecchini G: Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin. J Biol Chem. 1989 Aug 15;264(23):13599-604. [Article]
  6. Schroder I, Gunsalus RP, Ackrell BA, Cochran B, Cecchini G: Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis. J Biol Chem. 1991 Jul 25;266(21):13572-9. [Article]
  7. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  8. Yi X, Mroczko M, Manoj KM, Wang X, Hager LP: Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12412-7. [Article]
  9. Iverson TM, Luna-Chavez C, Cecchini G, Rees DC: Structure of the Escherichia coli fumarate reductase respiratory complex. Science. 1999 Jun 18;284(5422):1961-6. [Article]
  10. Iverson TM, Luna-Chavez C, Croal LR, Cecchini G, Rees DC: Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. J Biol Chem. 2002 May 3;277(18):16124-30. Epub 2002 Feb 15. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00730Thiabendazoleapproved, vet_approvedyesinhibitorDetails
DB074902-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOLexperimentalunknownDetails
DB079182-heptyl-4-hydroxyquinoline N-oxideexperimentalunknownDetails