ID   SDHA_COXBU              Reviewed;         587 AA.
AC   P51054;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Succinate dehydrogenase flavoprotein subunit;
DE            EC=1.3.5.1 {ECO:0000250|UniProtKB:P0AC41};
GN   Name=sdhA; OrderedLocusNames=CBU_1401;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Nine Mile;
RX   PubMed=7698664; DOI=10.1016/0378-1119(94)00888-y;
RA   Heinzen R.A., Mo Y.-Y., Robertson S.J., Mallavia L.P.;
RT   "Characterization of the succinate dehydrogenase-encoding gene cluster
RT   (sdh) from the rickettsia Coxiella burnetii.";
RL   Gene 155:27-34(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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 protein, cytochrome b-556 and a
CC       hydrophobic 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; L33409; AAA74133.1; -; Genomic_DNA.
DR   EMBL; AE016828; AAO90900.1; -; Genomic_DNA.
DR   PIR; I40849; I40849.
DR   RefSeq; NP_820386.1; NC_002971.3.
DR   RefSeq; WP_010958202.1; NC_002971.4.
DR   AlphaFoldDB; P51054; -.
DR   SMR; P51054; -.
DR   STRING; 227377.CBU_1401; -.
DR   PRIDE; P51054; -.
DR   DNASU; 1209307; -.
DR   EnsemblBacteria; AAO90900; AAO90900; CBU_1401.
DR   GeneID; 1209307; -.
DR   KEGG; cbu:CBU_1401; -.
DR   PATRIC; fig|227377.7.peg.1403; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_014312_6_1_6; -.
DR   OMA; DPIPIQP; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045282; C:plasma membrane succinate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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; Reference proteome; Transport;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..587
FT                   /note="Succinate dehydrogenase flavoprotein subunit"
FT                   /id="PRO_0000158651"
FT   ACT_SITE        288
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         15..20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         39..54
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         223
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         389
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         400
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         405..406
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   MOD_RES         47
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
SQ   SEQUENCE   587 AA;  65438 MW;  37B264ECC98D3DB6 CRC64;
     MSSIRVKQYD ALIVGAGGAG LRAALEMAQS RQYKVAVVSK VFPTRSHTVS AQGGIAAALG
     NVVPDKPIWH MFDTVKGSDY LGDQDAIQYM CEQAPPSVYE LEHYGLPFSR LDDGRIYQRA
     FGGHTRDFGK EMARRTCACA DRTGHAMLHT LYQKNVEAGT HFYYEWYGID LVRGAQGGIA
     GMIAMNMETS ELVFFKSRAT IFATGGAGRI YETTSNAYTN TGDGIGMVLR AGLPVQDMEF
     WQFHPTGIYG VGCLITEGAR GEGGYLINKD GERFMERYSP HLKDLDCRDV VARSILQEVM
     AGGGVGPKKD HVLLKLDHLG EKVLRERLPG IIELSEKFAN VDITKEPIPI LPTCHYMMGG
     IPTNIHGQAL TVDENGKDQI IEGLFAAGEC ACVSVHGANR LGTNSLLDLV VFGRAIGLHL
     EEALKTELKH RSENPDDIDA AIARLKRWEK PNNVENPALL RQEMRKAMSE DFGVFREEQK
     MKQGLERLQK LNERLQRAKL TDTSRTFNNA RIEALELDNL MEVSYATAVS AQQRTESRGA
     HSRYDYKERD DANWLKHTVY FRDGHIAYRP VNMKPKGMDP FPPKSRD