FRDA_WOLSU
ID FRDA_WOLSU Reviewed; 656 AA.
AC P17412;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Fumarate reductase flavoprotein subunit;
DE EC=1.3.5.4;
DE AltName: Full=Quinol-fumarate reductase flavoprotein subunit {ECO:0000303|PubMed:10586875};
DE Short=QFR flavoprotein subunit {ECO:0000303|PubMed:10586875};
GN Name=frdA; OrderedLocusNames=WS0831;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2244791; DOI=10.1007/bf00276536;
RA Lauterbach F., Koertner C., Albracht S.P., Unden G., Kroeger A.;
RT "The fumarate reductase operon of Wolinella succinogenes. Sequence and
RT expression of the frdA and frdB genes.";
RL Arch. Microbiol. 154:386-393(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9492313; DOI=10.1046/j.1432-1327.1998.2510418.x;
RA Simon J., Gross R., Ringel M., Schmidt E., Kroeger A.;
RT "Deletion and site-directed mutagenesis of the Wolinella succinogenes
RT fumarate reductase operon.";
RL Eur. J. Biochem. 251:418-426(1998).
RN [3]
RP SEQUENCE REVISION TO 281-289; 490 AND 593.
RA Simon J.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX PubMed=3609021; DOI=10.1111/j.1432-1033.1987.tb13536.x;
RA Lauterbach F., Kortner C., Tripier D., Unden G.;
RT "Cloning and expression of the genes of two fumarate reductase subunits
RT from Wolinella succinogenes.";
RL Eur. J. Biochem. 166:447-452(1987).
RN [6] {ECO:0007744|PDB:1QLB}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH FAD, SEQUENCE
RP REVISION TO 281-289, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10586875; DOI=10.1038/46483;
RA Lancaster C.R.D., Kroeger A., Auer M., Michel H.;
RT "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A
RT resolution.";
RL Nature 402:377-385(1999).
RN [7] {ECO:0007744|PDB:1E7P}
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAD, FUNCTION,
RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF ARG-301.
RX PubMed=11248702; DOI=10.1046/j.1432-1033.2001.02053.x;
RA Lancaster C.R.D., Gross R., Simon J.;
RT "A third crystal form of Wolinella succinogenes quinol:fumarate reductase
RT reveals domain closure at the site of fumarate reduction.";
RL Eur. J. Biochem. 268:1820-1827(2001).
CC -!- FUNCTION: The fumarate reductase enzyme complex is required for
CC fumarate respiration using formate or sulfide as electron donor.
CC {ECO:0000269|PubMed:11248702, ECO:0000269|PubMed:9492313}.
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 Evidence={ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000269|PubMed:10586875,
CC ECO:0000269|PubMed:11248702};
CC -!- SUBUNIT: Part of an enzyme complex containing three subunits: a
CC flavoprotein (frdA), an iron-sulfur protein (frdB), and diheme
CC cytochrome b (frdC). {ECO:0000269|PubMed:10586875,
CC ECO:0000269|PubMed:11248702}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305|PubMed:10586875}; Cytoplasmic side
CC {ECO:0000305|PubMed:10586875}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ000662; CAA04214.2; -; Genomic_DNA.
DR EMBL; BX571659; CAE09942.1; -; Genomic_DNA.
DR EMBL; M28294; AAA27586.1; -; Genomic_DNA.
DR PIR; B44954; B44954.
DR RefSeq; WP_011138739.1; NC_005090.1.
DR PDB; 1E7P; X-ray; 3.10 A; A/D/G/J=1-656.
DR PDB; 1QLB; X-ray; 2.33 A; A/D=1-656.
DR PDB; 2BS2; X-ray; 1.78 A; A/D=1-656.
DR PDB; 2BS3; X-ray; 2.19 A; A/D=1-656.
DR PDB; 2BS4; X-ray; 2.76 A; A/D=1-656.
DR PDBsum; 1E7P; -.
DR PDBsum; 1QLB; -.
DR PDBsum; 2BS2; -.
DR PDBsum; 2BS3; -.
DR PDBsum; 2BS4; -.
DR AlphaFoldDB; P17412; -.
DR SMR; P17412; -.
DR STRING; 273121.WS0831; -.
DR DrugBank; DB07669; 2,3-Dimethyl-1,4-naphthoquinone.
DR TCDB; 3.D.10.1.3; the prokaryotic succinate dehydrogenase (sdh) family.
DR PRIDE; P17412; -.
DR EnsemblBacteria; CAE09942; CAE09942; WS0831.
DR KEGG; wsu:WS0831; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_2_7; -.
DR OMA; FGYWRET; -.
DR OrthoDB; 153138at2; -.
DR BRENDA; 1.3.5.4; 6642.
DR EvolutionaryTrace; P17412; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
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; IPR003952; FRD_SDH_FAD_BS.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Electron transport; FAD;
KW Flavoprotein; Membrane; Oxidoreductase; Reference proteome;
KW Respiratory chain; Transport.
FT CHAIN 1..656
FT /note="Fumarate reductase flavoprotein subunit"
FT /id="PRO_0000158667"
FT ACT_SITE 257
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT ACT_SITE 273
FT /evidence="ECO:0000250|UniProtKB:P00363"
FT BINDING 13..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 42..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 49..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 393
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT BINDING 409..410
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3, ECO:0007744|PDB:2BS4"
FT MOD_RES 43
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000269|PubMed:10586875,
FT ECO:0000269|PubMed:11248702, ECO:0007744|PDB:1E7P,
FT ECO:0007744|PDB:1QLB, ECO:0007744|PDB:2BS2,
FT ECO:0007744|PDB:2BS3"
FT MUTAGEN 301
FT /note="R->E: No growth on fumarate, loss of FAD cofactor,
FT no enzyme activity."
FT /evidence="ECO:0000269|PubMed:11248702"
FT MUTAGEN 301
FT /note="R->K: No growth on fumarate, retains FAD cofactor,
FT 15-fold decreased enzmye activity in vitro."
FT /evidence="ECO:0000269|PubMed:11248702"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 83..102
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:1QLB"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 156..171
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1E7P"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 301..313
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:2BS4"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 343..351
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 408..430
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 437..456
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 463..477
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 484..501
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 515..539
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:1E7P"
FT STRAND 554..556
FT /evidence="ECO:0007829|PDB:2BS2"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:1E7P"
FT STRAND 577..582
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 585..587
FT /evidence="ECO:0007829|PDB:2BS2"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 607..625
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 630..637
FT /evidence="ECO:0007829|PDB:2BS2"
FT HELIX 644..646
FT /evidence="ECO:0007829|PDB:2BS2"
SQ SEQUENCE 656 AA; 72719 MW; BFEE6E8316F7F618 CRC64;
MKVQYCDSLV IGGGLAGLRA AVATQQKGLS TIVLSLIPVK RSHSAAAQGG MQASLGNSKM
SDGDNEDLHF MDTVKGSDWG CDQKVARMFV NTAPKAIREL AAWGVPWTRI HKGDRMAIIN
AQKTTITEED FRHGLIHSRD FGGTKKWRTC YTADATGHTM LFAVANECLK LGVSIQDRKE
AIALIHQDGK CYGAVVRDLV TGDIIAYVAK GTLIATGGYG RIYKNTTNAV VCEGTGTAIA
LETGIAQLGN MEAVQFHPTP LFPSGILLTE GCRGDGGILR DVDGHRFMPD YEPEKKELAS
RDVVSRRMIE HIRKGKGVQS PYGQHLWLDI SILGRKHIET NLRDVQEICE YFAGIDPAEK
WAPVLPMQHY SMGGIRTDYR GEAKLKGLFS AGEAACWDMH GFNRLGGNSV SEAVVAGMIV
GEYFAEHCAN TQVDLETKTL EKFVKGQEAY MKSLVESKGT EDVFKIKNRM KDVMDDNVGI
FRDGPHLEKA VKELEELYKK SKNVGIKNKR LHANPELEEA YRVPMMLKVA LCVAKGALDR
TESRGAHNRE DYPKRDDINW LNRTLASWPN PEQTLPTLEY EALDVNEMEI APGYRGYGAK
GNYIENPLSV KRQEEIDKIQ SELEAAGKDR HAIQEALMPY ELPAKYKARN ERLGDK
