FRDA_SHEON
ID FRDA_SHEON Reviewed; 596 AA.
AC P83223;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Fumarate reductase flavoprotein subunit;
DE EC=1.3.5.4;
DE AltName: Full=Flavocytochrome c;
DE Short=FL cyt;
DE Flags: Precursor;
GN OrderedLocusNames=SO_0970;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=MR-1;
RX PubMed=11425747; DOI=10.1128/aem.67.7.3236-3244.2001;
RA Tsapin A.I., Vandenberghe I., Nealson K.H., Scott J.H., Meyer T.E.,
RA Cusanovich M.A., Harada E., Kaizu T., Akutsu H., Leys D., Van Beeumen J.J.;
RT "Identification of a small tetraheme cytochrome c and a flavocytochrome c
RT as two of the principal soluble cytochromes c in Shewanella oneidensis
RT strain MR1.";
RL Appl. Environ. Microbiol. 67:3236-3244(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH FAD; HEMES;
RP FUMARATE AND SUCCINATE.
RC STRAIN=MR-1;
RX PubMed=10581551; DOI=10.1038/70051;
RA Leys D., Tsapin A.S., Nealson K.H., Meyer T.E., Cusanovich M.A.,
RA Van Beeumen J.J.;
RT "Structure and mechanism of the flavocytochrome c fumarate reductase of
RT Shewanella putrefaciens MR-1.";
RL Nat. Struct. Biol. 6:1113-1117(1999).
CC -!- FUNCTION: Catalyzes fumarate reduction using artificial electron donors
CC such as methyl viologen. The physiological reductant is unknown, but
CC evidence indicates that flavocytochrome c participates in electron
CC transfer from formate to fumarate and possibly also to trimethylamine
CC oxide (TMAO). This enzyme is essentially unidirectional (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + succinate = a quinol + fumarate;
CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.4;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10581551}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- INDUCTION: By anaerobiosis and fumarate. {ECO:0000269|PubMed:11425747}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the FAD-dependent
CC oxidoreductase 2 family. FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; AE014299; AAN54044.1; -; Genomic_DNA.
DR RefSeq; NP_716599.1; NC_004347.2.
DR RefSeq; WP_011071245.1; NZ_CP053946.1.
DR PDB; 1D4C; X-ray; 2.90 A; A/B/C/D=25-596.
DR PDB; 1D4D; X-ray; 2.50 A; A=25-596.
DR PDB; 1D4E; X-ray; 2.80 A; A=25-596.
DR PDBsum; 1D4C; -.
DR PDBsum; 1D4D; -.
DR PDBsum; 1D4E; -.
DR AlphaFoldDB; P83223; -.
DR SMR; P83223; -.
DR STRING; 211586.SO_0970; -.
DR DrugBank; DB00518; Albendazole.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB01677; Fumaric acid.
DR PaxDb; P83223; -.
DR KEGG; son:SO_0970; -.
DR PATRIC; fig|211586.12.peg.930; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_5_6; -.
DR OMA; EDLWVVV; -.
DR OrthoDB; 153138at2; -.
DR PhylomeDB; P83223; -.
DR BioCyc; SONE211586:G1GMP-903-MON; -.
DR EvolutionaryTrace; P83223; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010960; Flavocytochrome_c.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR012286; Tetrahaem_cytochrome.
DR Pfam; PF14537; Cytochrom_c3_2; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01813; flavo_cyto_c; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; FAD; Flavoprotein; Heme; Iron;
KW Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000305"
FT CHAIN 26..596
FT /note="Fumarate reductase flavoprotein subunit"
FT /id="PRO_0000010345"
FT REGION 142..596
FT /note="Flavoprotein-like"
FT ACT_SITE 426
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0C278"
FT BINDING 34
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 40
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 43
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 44
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 63
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 66
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 67
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 85
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 88
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 95
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 98
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 99
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 102
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 109
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 112
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 113
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 161
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4D"
FT BINDING 180..181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4D"
FT BINDING 188..195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4D"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4D"
FT BINDING 389
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4D"
FT BINDING 401..402
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4E"
FT BINDING 401..402
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4D"
FT BINDING 528
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4E"
FT BINDING 528
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4D"
FT BINDING 559
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4D"
FT BINDING 569
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4E"
FT BINDING 569
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4D"
FT BINDING 574..575
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10581551,
FT ECO:0007744|PDB:1D4D"
FT CONFLICT 71
FT /note="K -> E (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="A -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1D4D"
FT TURN 34..38
FT /evidence="ECO:0007829|PDB:1D4D"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1D4C"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:1D4D"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:1D4C"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:1D4D"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1D4D"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 277..291
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 295..307
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:1D4C"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:1D4D"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 344..350
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 368..375
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:1D4D"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 426..434
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 455..461
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 471..478
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 482..495
FT /evidence="ECO:0007829|PDB:1D4D"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 515..530
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:1D4D"
FT STRAND 541..556
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:1D4C"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:1D4D"
FT TURN 564..567
FT /evidence="ECO:0007829|PDB:1D4D"
FT HELIX 573..591
FT /evidence="ECO:0007829|PDB:1D4D"
SQ SEQUENCE 596 AA; 62448 MW; 74CB81FE89790463 CRC64;
MFTRKIQKTA LAMLISGAMA GTAYAAPEVL ADFHGEMGGC DSCHVSDKGG VTNDNLTHEN
GQCVSCHGDL KELAAAAPKD KVSPHKSHLI GEIACTSCHK GHEKSVAYCD ACHSFGFDMP
FGGKWERKFV PVDADKAAQD KAIAAGVKET TDVVIIGSGG AGLAAAVSAR DAGAKVILLE
KEPIPGGNTK LAAGGMNAAE TKPQAKLGIE DKKQIMIDDT MKGGRNINDP ELVKVLANNS
SDSIDWLTSM GADMTDVGRM GGASVNRSHR PTGGAGVGAH VAQVLWDNAV KRGTDIRLNS
RVVRILEDAS GKVTGVLVKG EYTGYYVIKA DAVVIAAGGF AKNNERVSKY DPKLKGFKAT
NHPGATGDGL DVALQAGAAT RDLEYIQAHP TYSPAGGVMI TEAVRGNGAI VVNREGNRFM
NEITTRDKAS AAILQQKGES AYLVFDDSIR KSLKAIEGYV HLNIVKEGKT IEELAKQIDV
PAAELAKTVT AYNGFVKSGK DAQFERPDLP RELVVAPFYA LEIAPAVHHT MGGLVIDTKA
EVKSEKTGKP ITGLYAAGEV TGGVHGANRL GGNAISDIVT YGRIAGASAA KFAKDN
