Fumarate reductase flavoprotein subunit
Details
- Name
- Fumarate reductase flavoprotein subunit
- Synonyms
- 1.3.5.4
- fcc3
- Flavocytochrome c
- Flavocytochrome c3
- Gene Name
- fccA
- Organism
- Shewanella frigidimarina
- Amino acid sequence
>lcl|BSEQ0016640|Fumarate reductase flavoprotein subunit ADNLAEFHVQNQECDSCHTPDGELSNDSLTYENTQCVSCHGTLEEVAETTKHEHYNAHAS HFPGEVACTSCHSAHEKSMVYCDSCHSFDFNMPYAKKWQRDEPTIAELAKDKSERQAALA SAPHDTVDVVVVGSGGAGFSAAISATDSGAKVILIEKEPVIGGNAKLAAGGMNAAWTDQQ KAKKITDSPELMFEDTMKGGQNINDPALVKVLSSHSKDSVDWMTAMGADLTDVGMMGGAS VNRAHRPTGGAGVGAHVVQVLYDNAVKRNIDLRMNTRGIEVLKDDKGTVKGILVKGMYKG YYWVKADAVILATGGFAKNNERVAKLDPSLKGFISTNQPGAVGDGLDVAENAGGALKDMQ YIQAHPTLSVKGGVMVTEAVRGNGAILVNREGKRFVNEITTRDKASAAILAQTGKSAYLI FDDSVRKSLSKIDKYIGLGVAPTADSLVKLGKMEGIDGKALTETVARYNSLVSSGKDTDF ERPNLPRALNEGNYYAIEVTPGVHHTMGGVMIDTKAEVMNAKKQVIPGLYGAGEVTGGVH GANRLGGNAISDIITFGRLAGEEAAKYSKKN
- Number of residues
- 571
- Molecular Weight
- 60620.95
- Theoretical pI
- 6.51
- GO Classification
- Functionselectron carrier activity / metal ion binding / succinate dehydrogenase activityProcessesanaerobic electron transport chain / anaerobic respirationComponentsouter membrane-bounded periplasmic space
- General Function
- Succinate dehydrogenase activity
- Specific Function
- Catalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). This enzyme is essentially unidirectional.
- Pfam Domain Function
- FAD_binding_2 (PF00890)
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0003961|1683 bp AACCAAGAATGTGATAGCTGCCATACACCAGATGGTGAACTGTCAAATGACAGCTTAACT TATGAAAATACACAATGTGTATCTTGCCATGGCACACTAGAGGAAGTCGCTGAAACGACA AAACATGAACACTATAATGCTCATGCTTCTCATTTCCCTGGCGAAGTAGCTTGTACCTCA TGCCACAGCGCACACGAAAAATCGATGGTGTATTGTGACTCTTGCCATAGCTTCGATTTC AACATGCCTTATGCTAAAAAATGGCAACGTGACGAGCCTACTATTGCTGAACTGGCCAAA GATAAATCAGAACGTCAGGCTGCTCTTGCTAGCGCACCTCACGATACTGTTGACGTAGTG GTTGTCGGTTCTGGCGGCGCAGGTTTCTCAGCAGCAATATCTGCAACAGACAGTGGTGCT AAAGTCATTCTTATTGAAAAAGAGCCTGTTATTGGTGGTAATGCTAAGTTAGCTGCGGGT GGCATGAACGCTGCTTGGACTGATCAACAAAAAGCCAAAAAAATTACTGACAGCCCAGAG TTAATGTTCGAAGACACCATGAAAGGTGGCCAAAACATAAATGATCCTGCATTAGTTAAA GTATTAAGCTCACACTCTAAAGACTCTGTTGATTGGATGACCGCTATGGGTGCCGATTTA ACTGATGTTGGCATGATGGGTGGCGCATCTGTTAATCGTGCGCATCGTCCAACCGGTGGT GCTGGTGTAGGTGCTCATGTTGTTCAAGTACTTTATGATAATGCAGTGAAACGCAATATC GACTTACGCATGAACACTCGCGGCATTGAAGTGCTTAAAGATGATAAAGGCACTGTTAAA GGTATTCTGGTTAAGGGTATGTATAAAGGTTACTACTGGGTGAAAGCCGATGCGGTAATC TTAGCAACGGGTGGTTTCGCTAAAAATAACGAGCGTGTCGCTAAGCTTGATCCTTCACTA AAAGGCTTTATCTCTACTAACCAACCTGGTGCAGTAGGTGATGGACTGGATGTAGCGGAA AATGCGGGCGGCGCATTGAAAGACATGCAGTATATCCAAGCTCACCCAACACTATCTGTT AAAGGTGGCGTAATGGTCACTGAAGCGGTTCGTGGTAATGGTGCGATTTTGGTTAACCGT GAAGGTAAGCGTTTCGTTAACGAAATTACTACTCGTGATAAAGCATCTGCCGCTATCTTA GCGCAAACCGGTAAATCAGCTTATTTGATTTTTGATGATTCTGTGCGTAAGTCACTGTCA AAAATTGATAAGTATATTGGTTTAGGTGTTGCACCAACCGCAGATAGCCTAGTTAAATTA GGTAAAATGGAAGGTATTGACGGCAAAGCATTGACTGAAACTGTCGCGCGTTACAACAGC TTAGTGAGTAGCGGTAAAGACACTGATTTTGAGCGTCCAAACCTACCGCGCGCACTTAAC GAAGGTAACTACTATGCAATTGAAGTTACACCTGGTGTTCACCACACTATGGGTGGCGTG ATGATCGACACTAAAGCTGAAGTCATGAATGCTAAGAAGCAGGTTATCCCTGGCTTGTAT GGTGCTGGTGAGGTTACTGGCGGTGTTCATGGTGCTAACCGCTTAGGTGGTAATGCTATT TCAGACATCATCACCTTCGGTCGCTTAGCGGGTGAAGAAGCTGCAAAATATTCTAAAAAG AAC
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0C278 UniProtKB Entry Name FRDA_SHEFR GenBank Protein ID 4539587 GenBank Gene ID AJ132010 - General References
- Pealing SL, Lysek DA, Taylor P, Alexeev D, Reid GA, Chapman SK, Walkinshaw MD: Crystallization and preliminary X-ray analysis of flavocytochrome c(3), the fumarate reductase from Shewanella frigidimarina. J Struct Biol. 1999 Aug;127(1):76-8. [Article]
- Taylor P, Pealing SL, Reid GA, Chapman SK, Walkinshaw MD: Structural and mechanistic mapping of a unique fumarate reductase. Nat Struct Biol. 1999 Dec;6(12):1108-12. [Article]
- Doherty MK, Pealing SL, Miles CS, Moysey R, Taylor P, Walkinshaw MD, Reid GA, Chapman SK: Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study. Biochemistry. 2000 Sep 5;39(35):10695-701. [Article]
- Mowat CG, Moysey R, Miles CS, Leys D, Doherty MK, Taylor P, Walkinshaw MD, Reid GA, Chapman SK: Kinetic and crystallographic analysis of the key active site acid/base arginine in a soluble fumarate reductase. Biochemistry. 2001 Oct 16;40(41):12292-8. [Article]
- Pankhurst KL, Mowat CG, Miles CS, Leys D, Walkinshaw MD, Reid GA, Chapman SK: Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina. Biochemistry. 2002 Jul 9;41(27):8551-6. [Article]
- Mowat CG, Pankhurst KL, Miles CS, Leys D, Walkinshaw MD, Reid GA, Chapman SK: Engineering water to act as an active site acid catalyst in a soluble fumarate reductase. Biochemistry. 2002 Oct 8;41(40):11990-6. [Article]
- Rothery EL, Mowat CG, Miles CS, Walkinshaw MD, Reid GA, Chapman SK: Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina. Biochemistry. 2003 Nov 18;42(45):13160-9. [Article]
- Rothery EL, Mowat CG, Miles CS, Mott S, Walkinshaw MD, Reid GA, Chapman SK: Probing domain mobility in a flavocytochrome. Biochemistry. 2004 May 4;43(17):4983-9. [Article]
- Pankhurst KL, Mowat CG, Rothery EL, Hudson JM, Jones AK, Miles CS, Walkinshaw MD, Armstrong FA, Reid GA, Chapman SK: A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina. J Biol Chem. 2006 Jul 21;281(29):20589-97. Epub 2006 May 12. [Article]