ID B9KF59_CAMLR Unreviewed; 663 AA.
AC B9KF59;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Fumarate reductase, flavoprotein subunit {ECO:0000313|EMBL:ACM63694.2};
DE EC=1.3.5.4 {ECO:0000313|EMBL:ACM63694.2};
GN Name=frdA {ECO:0000313|EMBL:ACM63694.2};
GN OrderedLocusNames=Cla_0334 {ECO:0000313|EMBL:ACM63694.2};
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263 {ECO:0000313|EMBL:ACM63694.2, ECO:0000313|Proteomes:UP000007727};
RN [1] {ECO:0000313|EMBL:ACM63694.2, ECO:0000313|Proteomes:UP000007727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060
RC {ECO:0000313|Proteomes:UP000007727};
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
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DR EMBL; CP000932; ACM63694.2; -; Genomic_DNA.
DR RefSeq; WP_041570261.1; NC_012039.1.
DR AlphaFoldDB; B9KF59; -.
DR STRING; 306263.Cla_0334; -.
DR GeneID; 7410242; -.
DR KEGG; cla:CLA_0334; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_2_7; -.
DR Proteomes; UP000007727; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR Gene3D; 3.10.20.820; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
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 NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR PANTHER; PTHR11632:SF71; FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACM63694.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007727};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 7..414
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 473..602
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 663 AA; 73822 MW; 4814ECB3538FD9A8 CRC64;
MNIQYSDALV IGGGLAGLRA AIEVAKSGQS VTLLSICPVK RSHSAAVQGG MQASLGNSVK
GEGDNEDVHF ADTVKGSDWG CDQEVARMFA QTAPKAVREL AAWGVPWTRV TKGPRTVVIN
AQKTTIEEKE EAHGLINARD FGGTKKWRTC YIADATGHCM LYGVANEAIK HQVKIIDRME
AVRIIHDGKK CLGAIARDLT NGELIAYVAR GTMIATGGYG RIYKQTTNAV ICEGTGAAIA
LETGLCRLSN MEAVQFHPTP IVPSGILLTE GCRGDGGILR DVDGYRFMPD YEPEKKELAS
RDVVSRRMME HIRKGKGVKS PYGDHLWLDI SILGRAHVEK NLRDVQDICK TFNGIDPADE
GPKGWAPVLP MQHYSMGGIR TKPTGESQWL NGLFACGEAA CWDMHGFNRL GGNSCSETVV
AGMIVGDYFA QYCKENGNDI DTNIVKSFLS KEYDYLKSLV SKEGKHDVFE IKNRMKDIMW
EKVAIFRTGQ GLEEAVKELE ELYQKSLDLK VHDKELKCAN PELEEAYRVP RMLKIALCVA
YGALLRTESR GAHYREDYPK RDDLNWMKRT NTYWVEGESM PRVEYEDLDI MKMEIPPAFR
GYGAKGNIIE NPLSEKRQAE VDAIREKMES EGKGRYEIQH ALMPYELQAK FKAPNQRIGV
DYE
//
