FRDA_SHEFN
ID FRDA_SHEFN Reviewed; 596 AA.
AC Q07WU7; Q02469; Q9X969;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Fumarate reductase flavoprotein subunit;
DE EC=1.3.5.4;
DE AltName: Full=Flavocytochrome c;
DE AltName: Full=Flavocytochrome c3;
DE Short=Fcc3;
DE Flags: Precursor;
GN Name=fccA; Synonyms=fcc3; OrderedLocusNames=Sfri_3690;
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], AND PROTEIN SEQUENCE OF 26-38.
RX PubMed=1333793; DOI=10.1021/bi00163a023;
RA Pealing S.L., Black A.C., Manson F.D.C., Ward F.B., Chapman S.K.,
RA Reid G.A.;
RT "Sequence of the gene encoding flavocytochrome c from Shewanella
RT putrefaciens: a tetraheme flavoenzyme that is a soluble fumarate reductase
RT related to the membrane-bound enzymes from other bacteria.";
RL Biochemistry 31:12132-12140(1992).
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.
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; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- INDUCTION: By anaerobiosis and fumarate.
CC -!- SIMILARITY: In the C-terminal section; belongs to the FAD-dependent
CC oxidoreductase 2 family. FRD/SDH subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI73517.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L04283; AAA70385.1; -; Genomic_DNA.
DR EMBL; CP000447; ABI73517.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041413240.1; NC_008345.1.
DR AlphaFoldDB; Q07WU7; -.
DR SMR; Q07WU7; -.
DR STRING; 318167.Sfri_3690; -.
DR EnsemblBacteria; ABI73517; ABI73517; Sfri_3690.
DR KEGG; sfr:Sfri_3690; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_5_6; -.
DR OrthoDB; 153138at2; -.
DR SABIO-RK; Q07WU7; -.
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 InterPro; IPR013087; Znf_C2H2_type.
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 Direct protein sequencing; Electron transport; FAD; Flavoprotein; Heme;
KW Iron; Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:1333793"
FT CHAIN 26..596
FT /note="Fumarate reductase flavoprotein subunit"
FT /id="PRO_0000269231"
FT REGION 143..596
FT /note="Flavoprotein-like"
FT ACT_SITE 427
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 33
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 39
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 42
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 /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 61
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 64
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 65
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 83
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 86
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 93
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 96
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 97
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 100
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 107
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 110
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 111
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 154..168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 157..168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 181..182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 189..190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 194..196
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 402..403
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000250|UniProtKB:P83223"
FT BINDING 529
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000250|UniProtKB:P83223"
FT BINDING 569
FT /ligand="fumarate"
FT /ligand_id="ChEBI:CHEBI:29806"
FT /evidence="ECO:0000250|UniProtKB:P83223"
FT BINDING 574..575
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 596 AA; 63027 MW; 914B69FD502BAC5B CRC64;
MKKMNLAVCI ATLMGTAGLM GTAVAADNLA EFHVQNQECD SCHTPDGELS NDSLTYENTQ
CVSCHGTLAE VAETTKHEHY NAHASHFPGE VACTSCHSAH EKSMVYCDSC HSFDFNMPYA
KKWLRDEPTI AELAKDKSER QAALASAPHD TVDVVVVGSG GAGFSAAISA TDSGAKVILI
EKEPVIGGNA KLAAGGMNAA WTDQQKAKKI TDSPELMFED TMKGGQNIND PALVKVLSSH
SKDSVDWMTA MGADLTDVGM MGGASVNRAH RPTGGAGVGA HVVQVLYDNA VKRNIDLRMN
TRGIEVLKDD KGTVKGILVK GMYKGYYWVK ADAVILATGG FAKNNERVAK LDPSLKGFIS
TNQPGAVGDG LDVAENAGGA LKDMQYIQAH PTLSVKGGVM VTEAVRGNGA ILVNREGKRF
VNEITTRDKA SAAILAQTGK SAYLIFDDSV RKSLSKIDKY IGLGVAPTAD SLVKLGKMEG
IDGKALTETV ARYNSLVSSG KDTDFERPNL PRALNEGNYY AIEVTPGVHH TMGGVMIDTK
AEVMNAKKQV IPGLYGAGEV TGGVHGANRL GGNAISDIIT FGRLAGEEAA KYSKKN
