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SDHA_RICFE
ID   SDHA_RICFE              Reviewed;         596 AA.
AC   Q4UJM1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Succinate dehydrogenase flavoprotein subunit;
DE            EC=1.3.5.1 {ECO:0000250|UniProtKB:P0AC41};
GN   Name=sdhA; OrderedLocusNames=RF_1159;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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=1.3.5.1;
CC         Evidence={ECO:0000250|UniProtKB:P0AC41};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P0AC41};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (bacterial route): step 1/1.
CC       {ECO:0000250|UniProtKB:P0AC41}.
CC   -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC       flavoprotein, an iron-sulfur, cytochrome b-556, and a hydrophobic
CC       anchor protein. {ECO:0000250|UniProtKB:P0AC41}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0AC41}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P0AC41}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P0AC41}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
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DR   EMBL; CP000053; AAY62010.1; -; Genomic_DNA.
DR   RefSeq; WP_011271467.1; NC_007109.1.
DR   AlphaFoldDB; Q4UJM1; -.
DR   SMR; Q4UJM1; -.
DR   STRING; 315456.RF_1159; -.
DR   EnsemblBacteria; AAY62010; AAY62010; RF_1159.
DR   KEGG; rfe:RF_1159; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_014312_6_1_5; -.
DR   OMA; DPIPIQP; -.
DR   OrthoDB; 153138at2; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000008548; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; IPR011281; Succ_DH_flav_su_fwd.
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; TIGR01816; sdhA_forward; 1.
DR   TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Electron transport; FAD; Flavoprotein;
KW   Membrane; Oxidoreductase; Transport; Tricarboxylic acid cycle.
FT   CHAIN           1..596
FT                   /note="Succinate dehydrogenase flavoprotein subunit"
FT                   /id="PRO_0000280977"
FT   ACT_SITE        290
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         18..23
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         41..56
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         225
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         391
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         402
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         407..408
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   MOD_RES         49
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
SQ   SEQUENCE   596 AA;  65130 MW;  9AF860F6EEFEB3E1 CRC64;
     MTKAYNIIHH KFDVVVVGAG GAGLRSAFGM AKEGLNTACI TKLFPTRSHT VAAQGGISAA
     LGNMGEDDWR WHMYDTVKGS DWLGDQDAIE YMCKNAPDAI LELEHYGVPF SRTEEGKIYQ
     RPFGGMTTEY GKGKAAQRTC AAADRTGHAI LHTLYQQSLK HKVQFFVEYF AIDLLMEDGE
     CRGVVVWNLD DGTLHCFRAH NVVLATGGYG RAYFSATSAH TCTGDGGGMA IRAGLPLQDM
     EFVQFHPTGI YSAGCLITEG ARGEGGYLVN ANGERFMERY APAAKDLASR DVVSRAMTIE
     IREGRGVGEH KDHVFLHLNH LSPEILHSRL PGISETAKIF AGVDVTKEPI PVLPTVHYNM
     GGIPTNYHGQ VIIKDGTNHN SVVKGLMAIG EAACVSVHGA NRLGSNSLLD LVVFGRSSAL
     KAAELISPAS PHKPIKEASL EKIINRFDKV RHANGNILVA DLRLKMQRTM QSHASVFRTQ
     EVLDEGAGMI SEIRNGYKDI KINDKSLIWN SDLVEALELD NLLDQALVTV YSAAARKESR
     GAHAREDYPD RNDGDWMKHT LSSIDEAGKI VIDYKPVTLT TLTDEISAIP PAKRVY
 
 
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