Fumarate reductase flavoprotein subunit

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	None
Molecular Weight	60620.95
Theoretical pI	6.51
GO Classification	Functions metal ion binding succinate dehydrogenase activity electron carrier activity Processes anaerobic respiration anaerobic electron transport chain Components outer 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.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P0C278
UniProtKB Entry Name
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
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
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. [10479620 ] 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. [10581550 ] 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. [10978153 ] 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. [11591148 ] 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. [12093271 ] 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. [12356299 ] 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. [14609326 ] 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. [15109257 ] 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. [16699170 ]

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