FRD2_SHEFN
ID FRD2_SHEFN Reviewed; 588 AA.
AC Q9Z4P0; Q07ZY8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Fumarate reductase flavoprotein subunit;
DE EC=1.3.5.4;
DE AltName: Full=Fe(3+)-induced flavocytochrome C3;
DE Short=Ifc3;
DE AltName: Full=Iron(III)-induced flavocytochrome C3;
DE Flags: Precursor;
GN Name=ifcA; OrderedLocusNames=Sfri_2586;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-32; 190-199 AND
RP 215-229, CHARACTERIZATION, AND MASS SPECTROMETRY.
RX PubMed=10455032; DOI=10.1042/bj3420439;
RA Dobbin P.S., Butt J.N., Powell A.K., Reid G.A., Richardson D.J.;
RT "Characterization of a flavocytochrome that is induced during the anaerobic
RT respiration of Fe3+ by Shewanella frigidimarina NCIMB400.";
RL Biochem. J. 342:439-448(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RX PubMed=10581549; DOI=10.1038/70039;
RA Bamford V., Dobbin P.S., Richardson D.J., Hemmings A.M.;
RT "Open conformation of a flavocytochrome c3 fumarate reductase.";
RL Nat. Struct. Biol. 6:1104-1107(1999).
CC -!- FUNCTION: Catalyzes unidirectional fumarate reduction using artificial
CC electron donors such as methyl viologen. The physiological reductant is
CC unknown.
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: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By anaerobic growth on Fe(3+) ions.
CC -!- MASS SPECTROMETRY: Mass=63985; Mass_error=0.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10455032};
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; AJ236923; CAB37062.1; -; Genomic_DNA.
DR EMBL; CP000447; ABI72427.1; -; Genomic_DNA.
DR RefSeq; WP_011638036.1; NC_008345.1.
DR PDB; 1QO8; X-ray; 2.15 A; A/D=23-588.
DR PDBsum; 1QO8; -.
DR AlphaFoldDB; Q9Z4P0; -.
DR SMR; Q9Z4P0; -.
DR STRING; 318167.Sfri_2586; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR EnsemblBacteria; ABI72427; ABI72427; Sfri_2586.
DR KEGG; sfr:Sfri_2586; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_5_6; -.
DR OMA; RLMGNAL; -.
DR OrthoDB; 153138at2; -.
DR EvolutionaryTrace; Q9Z4P0; -.
DR Proteomes; UP000000684; 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; Direct protein sequencing; Electron transport; FAD;
KW Flavoprotein; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:10455032"
FT CHAIN 23..588
FT /note="Fumarate reductase flavoprotein subunit"
FT /id="PRO_0000010346"
FT REGION 135..588
FT /note="Flavoprotein-like"
FT ACT_SITE 382
FT /evidence="ECO:0000250"
FT ACT_SITE 398
FT /evidence="ECO:0000250"
FT BINDING 31
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 37
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 40
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 41
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 58
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 61
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 62
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 78
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 81
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 87
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 90
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 91
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 94
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 101
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 104
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 105
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 146..160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 394..395
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000250|UniProtKB:P83223"
FT BINDING 521
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000250|UniProtKB:P83223"
FT BINDING 561
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000250|UniProtKB:P83223"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1QO8"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:1QO8"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 223..242
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 304..313
FT /evidence="ECO:0007829|PDB:1QO8"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 317..328
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 337..343
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 379..389
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 419..427
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 434..439
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 440..445
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 447..454
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 464..470
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 475..491
FT /evidence="ECO:0007829|PDB:1QO8"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 508..523
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 542..548
FT /evidence="ECO:0007829|PDB:1QO8"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:1QO8"
FT HELIX 565..585
FT /evidence="ECO:0007829|PDB:1QO8"
SQ SEQUENCE 588 AA; 62946 MW; 99C4AE25814693D2 CRC64;
MKLKYLVSAM ALVVLSSGTA MAKTPDMGSF HADMGSCQSC HAKPIKVTDS ETHENAQCKS
CHGEYAELAN DKLQFDPHNS HLGDINCTSC HKGHEEPKFY CNECHSFDIK PMPFSDAKKK
KSWDDGWDQD KIQKAIAAGP SETTQVLVVG AGSAGFNASL AAKKAGANVI LVDKAPFSGG
NSMISAGGMN AVGTKQQTAH GVEDKVEWFI EDAMKGGRQQ NDIKLVTILA EQSADGVQWL
ESLGANLDDL KRSGGARVDR THRPHGGKSS GPEIIDTLRK AAKEQGIDTR LNSRVVKLVV
NDDHSVVGAV VHGKHTGYYM IGAKSVVLAT GGYGMNKEMI AYYRPTMKDM TSSNNITATG
DGVLMAKEIG ASMTDIDWVQ AHPTVGKDSR ILISETVRGV GAVMVNKDGN RFISELTTRD
KASDAILKQP GQFAWIIFDN QLYKKAKMVR GYDHLEMLYK GDTVEQLAKS TGMKVADLAK
TVSDYNGYVA SGKDTAFGRA DMPLNMTQSP YYAVKVAPGI HHTMGGVAIN TTASVLDLQS
KPIDGLFAAG EVTGGVHGYN RLGGNAIADT VVFGRIAGDN AAKHALDK
