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Fumarate reductase flavoprotein subunit (EC 1.3.5.4) (Flavocytochrome c) (Flavocytochrome c3) (Fcc3)

 FRDA_SHEFR              Reviewed;         571 AA.
P0C278; Q02469; Q9X969;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 1.
28-FEB-2018, entry version 59.
RecName: Full=Fumarate reductase flavoprotein subunit;
EC=1.3.5.4;
AltName: Full=Flavocytochrome c;
AltName: Full=Flavocytochrome c3;
Short=Fcc3;
Name=fccA; Synonyms=fcc3;
Shewanella frigidimarina.
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Shewanellaceae; Shewanella.
NCBI_TaxID=56812;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-571, AND CRYSTALLIZATION.
STRAIN=ACAM591;
PubMed=10479620; DOI=10.1006/jsbi.1999.4139;
Pealing S.L., Lysek D.A., Taylor P., Alexeev D., Reid G.A.,
Chapman S.K., Walkinshaw M.D.;
"Crystallization and preliminary X-ray analysis of flavocytochrome
c(3), the fumarate reductase from Shewanella frigidimarina.";
J. Struct. Biol. 127:76-78(1999).
[2]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=10581550; DOI=10.1038/70045;
Taylor P., Pealing S.L., Reid G.A., Chapman S.K., Walkinshaw M.D.;
"Structural and mechanistic mapping of a unique fumarate reductase.";
Nat. Struct. Biol. 6:1108-1112(1999).
[3]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-365 AND ALA-504
IN COMPLEX WITH FAD; FUMARATE AND HEMES, AND MUTAGENESIS OF HIS-365;
ARG-402 AND HIS-504.
PubMed=10978153; DOI=10.1021/bi000871l;
Doherty M.K., Pealing S.L., Miles C.S., Moysey R., Taylor P.,
Walkinshaw M.D., Reid G.A., Chapman S.K.;
"Identification of the active site acid/base catalyst in a bacterial
fumarate reductase: a kinetic and crystallographic study.";
Biochemistry 39:10695-10701(2000).
[4]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA-402; LYS-402 AND
TYR-402, MUTAGENESIS OF ARG-402, AND ENZYME KINETICS.
PubMed=11591148; DOI=10.1021/bi011360h;
Mowat C.G., Moysey R., Miles C.S., Leys D., Doherty M.K., Taylor P.,
Walkinshaw M.D., Reid G.A., Chapman S.K.;
"Kinetic and crystallographic analysis of the key active site
acid/base arginine in a soluble fumarate reductase.";
Biochemistry 40:12292-12298(2001).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-505 AND TYR-505,
AND CHARACTERIZATION.
PubMed=12093271; DOI=10.1021/bi020155e;
Pankhurst K.L., Mowat C.G., Miles C.S., Leys D., Walkinshaw M.D.,
Reid G.A., Chapman S.K.;
"Role of His505 in the soluble fumarate reductase from Shewanella
frigidimarina.";
Biochemistry 41:8551-8556(2002).
[6]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS PHE-363 AND
PHE-363/ALA-402, CHARACTERIZATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=12356299; DOI=10.1021/bi0203177;
Mowat C.G., Pankhurst K.L., Miles C.S., Leys D., Walkinshaw M.D.,
Reid G.A., Chapman S.K.;
"Engineering water to act as an active site acid catalyst in a soluble
fumarate reductase.";
Biochemistry 41:11990-11996(2002).
[7]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS ALA-61 AND MET-61 IN
COMPLEXES WITH HEME; SUBSTRATE AND FAD, MASS SPECTROMETRY, AND
MUTAGENESIS OF HIS-61.
PubMed=14609326; DOI=10.1021/bi030159z;
Rothery E.L., Mowat C.G., Miles C.S., Walkinshaw M.D., Reid G.A.,
Chapman S.K.;
"Histidine 61: an important heme ligand in the soluble fumarate
reductase from Shewanella frigidimarina.";
Biochemistry 42:13160-13169(2003).
[8]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANT CYS-251/CYS430.
PubMed=15109257; DOI=10.1021/bi030261w;
Rothery E.L., Mowat C.G., Miles C.S., Mott S., Walkinshaw M.D.,
Reid G.A., Chapman S.K.;
"Probing domain mobility in a flavocytochrome.";
Biochemistry 43:4983-4989(2004).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ASP-378 AND MET-381,
MUTAGENESIS OF GLU-378 AND ARG-381, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16699170; DOI=10.1074/jbc.M603077200;
Pankhurst K.L., Mowat C.G., Rothery E.L., Hudson J.M., Jones A.K.,
Miles C.S., Walkinshaw M.D., Armstrong F.A., Reid G.A., Chapman S.K.;
"A proton delivery pathway in the soluble fumarate reductase from
Shewanella frigidimarina.";
J. Biol. Chem. 281:20589-20597(2006).
-!- 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.
-!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD per subunit.;
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10978153}.
-!- SUBCELLULAR LOCATION: Periplasm.
-!- INDUCTION: By anaerobiosis and fumarate.
-!- MASS SPECTROMETRY: Mass=63033; Mass_error=10; Method=Electrospray;
Range=1-571; Evidence={ECO:0000269|PubMed:14609326};
-!- SIMILARITY: In the C-terminal section; belongs to the FAD-
dependent oxidoreductase 2 family. FRD/SDH subfamily.
{ECO:0000305}.
-!- CAUTION: The N-terminal sequence has been extracted from PDB entry
1LJ1. {ECO:0000305}.
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EMBL; AJ132010; CAB38558.1; -; Genomic_DNA.
PDB; 1E39; X-ray; 1.80 A; A=1-571.
PDB; 1JRX; X-ray; 2.00 A; A/B=1-571.
PDB; 1JRY; X-ray; 2.00 A; A/B=1-571.
PDB; 1JRZ; X-ray; 2.00 A; A/B=1-571.
PDB; 1KSS; X-ray; 1.80 A; A=1-571.
PDB; 1KSU; X-ray; 2.00 A; A/B=1-571.
PDB; 1LJ1; X-ray; 2.00 A; A/B=1-571.
PDB; 1M64; X-ray; 1.80 A; A/B=1-571.
PDB; 1P2E; X-ray; 2.20 A; A=1-571.
PDB; 1P2H; X-ray; 2.10 A; A=1-571.
PDB; 1Q9I; X-ray; 1.60 A; A=1-571.
PDB; 1QJD; X-ray; 1.80 A; A=1-571.
PDB; 1Y0P; X-ray; 1.50 A; A=1-571.
PDB; 2B7R; X-ray; 1.70 A; A=1-571.
PDB; 2B7S; X-ray; 2.12 A; A=1-571.
PDBsum; 1E39; -.
PDBsum; 1JRX; -.
PDBsum; 1JRY; -.
PDBsum; 1JRZ; -.
PDBsum; 1KSS; -.
PDBsum; 1KSU; -.
PDBsum; 1LJ1; -.
PDBsum; 1M64; -.
PDBsum; 1P2E; -.
PDBsum; 1P2H; -.
PDBsum; 1Q9I; -.
PDBsum; 1QJD; -.
PDBsum; 1Y0P; -.
PDBsum; 2B7R; -.
PDBsum; 2B7S; -.
ProteinModelPortal; P0C278; -.
SMR; P0C278; -.
DrugBank; DB04734; Citraconic acid.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB01677; Fumarate.
DrugBank; DB03343; Malate Like Intermediate.
eggNOG; COG1053; LUCA.
SABIO-RK; P0C278; -.
EvolutionaryTrace; P0C278; -.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; NAS:UniProtKB.
GO; GO:0009055; F:electron transfer activity; NAS:UniProtKB.
GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
GO; GO:0019645; P:anaerobic electron transport chain; NAS:UniProtKB.
GO; GO:0009061; P:anaerobic respiration; NAS:UniProtKB.
Gene3D; 3.50.50.60; -; 2.
Gene3D; 3.90.700.10; -; 1.
InterPro; IPR003953; FAD-binding_2.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR010960; Flavocytochrome_c.
InterPro; IPR011031; Multihaem_cyt.
InterPro; IPR036280; Multihaem_cyt_sf.
InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
InterPro; IPR012286; Tetrahaem_cytochrome.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF14537; Cytochrom_c3_2; 1.
Pfam; PF00890; FAD_binding_2; 1.
SUPFAM; SSF48695; SSF48695; 1.
SUPFAM; SSF51905; SSF51905; 2.
SUPFAM; SSF56425; SSF56425; 1.
TIGRFAMs; TIGR01813; flavo_cyto_c; 1.
PROSITE; PS51008; MULTIHEME_CYTC; 1.
1: Evidence at protein level;
3D-structure; Electron transport; FAD; Flavoprotein; Heme; Iron;
Metal-binding; Oxidoreductase; Periplasm; Transport.
CHAIN 1 571 Fumarate reductase flavoprotein subunit.
/FTId=PRO_0000010344.
DOMAIN 1 117 Cytochrome c.
NP_BIND 132 143 FAD. {ECO:0000269|PubMed:10978153}.
NP_BIND 156 157 FAD. {ECO:0000269|PubMed:10978153}.
NP_BIND 164 165 FAD. {ECO:0000269|PubMed:10978153}.
NP_BIND 169 171 FAD. {ECO:0000269|PubMed:10978153}.
NP_BIND 549 550 FAD. {ECO:0000269|PubMed:10978153}.
REGION 118 571 Flavoprotein-like.
ACT_SITE 402 402 Proton donor.
METAL 8 8 Iron (heme 2 axial ligand).
METAL 18 18 Iron (heme 1 axial ligand).
METAL 40 40 Iron (heme 2 axial ligand).
METAL 58 58 Iron (heme 3 axial ligand).
METAL 61 61 Iron (heme 4 axial ligand).
METAL 72 72 Iron (heme 3 axial ligand).
METAL 75 75 Iron (heme 1 axial ligand).
METAL 86 86 Iron (heme 4 axial ligand).
BINDING 14 14 Heme 1 (covalent).
BINDING 17 17 Heme 1 (covalent).
BINDING 36 36 Heme 2 (covalent).
BINDING 39 39 Heme 2 (covalent).
BINDING 68 68 Heme 3 (covalent).
BINDING 71 71 Heme 3 (covalent).
BINDING 82 82 Heme 4 (covalent).
BINDING 85 85 Heme 4 (covalent).
BINDING 365 365 Substrate.
BINDING 377 377 Substrate.
BINDING 504 504 Substrate.
BINDING 544 544 Substrate.
MUTAGEN 61 61 H->A: Reduces catalytic activity 10-fold.
Reduces affinity for fumarate.
{ECO:0000269|PubMed:14609326}.
MUTAGEN 61 61 H->M: Reduces catalytic activity 5-fold.
Reduces affinity for fumarate.
{ECO:0000269|PubMed:14609326}.
MUTAGEN 365 365 H->A: Reduces catalytic activity by over
75%. {ECO:0000269|PubMed:10978153}.
MUTAGEN 378 378 E->D: Strongly reduced affinity for
substrate. Reduces activity 10000-fold.
{ECO:0000269|PubMed:16699170}.
MUTAGEN 381 381 R->M: Strongly reduced catalytic
activity. No effect on substrate
affinity. {ECO:0000269|PubMed:16699170}.
MUTAGEN 402 402 R->A: Loss of activity.
{ECO:0000269|PubMed:10978153,
ECO:0000269|PubMed:11591148}.
MUTAGEN 402 402 R->K,Y: Reduces activity 10000-fold.
{ECO:0000269|PubMed:10978153,
ECO:0000269|PubMed:11591148}.
MUTAGEN 504 504 H->A: Reduces catalytic activity by over
64%. {ECO:0000269|PubMed:10978153}.
HELIX 4 9 {ECO:0000244|PDB:1Y0P}.
HELIX 14 16 {ECO:0000244|PDB:1Y0P}.
HELIX 30 40 {ECO:0000244|PDB:1Y0P}.
HELIX 43 47 {ECO:0000244|PDB:1Y0P}.
TURN 57 59 {ECO:0000244|PDB:1P2H}.
HELIX 68 70 {ECO:0000244|PDB:1Y0P}.
STRAND 74 76 {ECO:0000244|PDB:1Y0P}.
HELIX 81 84 {ECO:0000244|PDB:1Y0P}.
HELIX 107 111 {ECO:0000244|PDB:1Y0P}.
HELIX 112 120 {ECO:0000244|PDB:1Y0P}.
STRAND 124 126 {ECO:0000244|PDB:1Y0P}.
STRAND 128 132 {ECO:0000244|PDB:1Y0P}.
HELIX 136 147 {ECO:0000244|PDB:1Y0P}.
STRAND 152 155 {ECO:0000244|PDB:1Y0P}.
STRAND 157 161 {ECO:0000244|PDB:1Y0P}.
HELIX 165 167 {ECO:0000244|PDB:1Y0P}.
HELIX 178 182 {ECO:0000244|PDB:1Y0P}.
HELIX 189 199 {ECO:0000244|PDB:1Y0P}.
TURN 200 202 {ECO:0000244|PDB:1Y0P}.
HELIX 206 225 {ECO:0000244|PDB:1Y0P}.
STRAND 232 234 {ECO:0000244|PDB:1Y0P}.
STRAND 244 247 {ECO:0000244|PDB:1Y0P}.
TURN 248 250 {ECO:0000244|PDB:1Y0P}.
HELIX 253 267 {ECO:0000244|PDB:1Y0P}.
STRAND 271 283 {ECO:0000244|PDB:1Y0P}.
STRAND 289 296 {ECO:0000244|PDB:1Y0P}.
TURN 297 299 {ECO:0000244|PDB:1Y0P}.
STRAND 300 305 {ECO:0000244|PDB:1Y0P}.
STRAND 307 311 {ECO:0000244|PDB:1Y0P}.
HELIX 320 326 {ECO:0000244|PDB:1Y0P}.
HELIX 328 330 {ECO:0000244|PDB:1Y0P}.
STRAND 335 337 {ECO:0000244|PDB:1JRX}.
HELIX 344 351 {ECO:0000244|PDB:1Y0P}.
STRAND 356 358 {ECO:0000244|PDB:1P2H}.
STRAND 362 369 {ECO:0000244|PDB:1Y0P}.
TURN 370 372 {ECO:0000244|PDB:1Y0P}.
STRAND 373 375 {ECO:0000244|PDB:1P2H}.
HELIX 379 382 {ECO:0000244|PDB:1Y0P}.
STRAND 386 388 {ECO:0000244|PDB:1Y0P}.
HELIX 402 410 {ECO:0000244|PDB:1Y0P}.
HELIX 413 415 {ECO:0000244|PDB:1Y0P}.
STRAND 417 422 {ECO:0000244|PDB:1Y0P}.
HELIX 423 428 {ECO:0000244|PDB:1Y0P}.
HELIX 432 438 {ECO:0000244|PDB:1Y0P}.
STRAND 443 446 {ECO:0000244|PDB:1Y0P}.
HELIX 447 454 {ECO:0000244|PDB:1Y0P}.
HELIX 458 474 {ECO:0000244|PDB:1Y0P}.
TURN 478 480 {ECO:0000244|PDB:1Y0P}.
STRAND 494 506 {ECO:0000244|PDB:1Y0P}.
STRAND 509 512 {ECO:0000244|PDB:1Y0P}.
STRAND 517 519 {ECO:0000244|PDB:1Y0P}.
STRAND 525 531 {ECO:0000244|PDB:1Y0P}.
STRAND 536 540 {ECO:0000244|PDB:1Y0P}.
HELIX 548 567 {ECO:0000244|PDB:1Y0P}.
SEQUENCE 571 AA; 60621 MW; D2E4FC43C9A6484C CRC64;
ADNLAEFHVQ NQECDSCHTP DGELSNDSLT YENTQCVSCH GTLEEVAETT KHEHYNAHAS
HFPGEVACTS CHSAHEKSMV YCDSCHSFDF NMPYAKKWQR DEPTIAELAK DKSERQAALA
SAPHDTVDVV VVGSGGAGFS AAISATDSGA KVILIEKEPV IGGNAKLAAG GMNAAWTDQQ
KAKKITDSPE LMFEDTMKGG QNINDPALVK VLSSHSKDSV DWMTAMGADL TDVGMMGGAS
VNRAHRPTGG AGVGAHVVQV LYDNAVKRNI DLRMNTRGIE VLKDDKGTVK GILVKGMYKG
YYWVKADAVI LATGGFAKNN ERVAKLDPSL KGFISTNQPG AVGDGLDVAE NAGGALKDMQ
YIQAHPTLSV KGGVMVTEAV RGNGAILVNR EGKRFVNEIT TRDKASAAIL AQTGKSAYLI
FDDSVRKSLS KIDKYIGLGV APTADSLVKL GKMEGIDGKA LTETVARYNS LVSSGKDTDF
ERPNLPRALN EGNYYAIEVT PGVHHTMGGV MIDTKAEVMN AKKQVIPGLY GAGEVTGGVH
GANRLGGNAI SDIITFGRLA GEEAAKYSKK N


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