SDHA_RICCN
ID SDHA_RICCN Reviewed; 596 AA.
AC Q92J97;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Succinate dehydrogenase flavoprotein subunit;
DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P0AC41};
GN Name=sdhA; OrderedLocusNames=RC0170;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL02708.1; -; Genomic_DNA.
DR PIR; B97721; B97721.
DR RefSeq; WP_010976845.1; NC_003103.1.
DR AlphaFoldDB; Q92J97; -.
DR SMR; Q92J97; -.
DR EnsemblBacteria; AAL02708; AAL02708; RC0170.
DR KEGG; rco:RC0170; -.
DR PATRIC; fig|272944.4.peg.199; -.
DR HOGENOM; CLU_014312_6_1_5; -.
DR OMA; DPIPIQP; -.
DR UniPathway; UPA00223; UER01005.
DR Proteomes; UP000000816; 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_0000158656"
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; 65291 MW; F313CE9506A7DA10 CRC64;
MTKAYNIIHH KFDVVVVGAG GAGLRSAFGM AKEGLNTACI TKLFPTRSHT VAAQGGISAA
LGNMGEDDWR WHMYDTVKGS DWLGDQDAIE YMCKNAPDAI LELEHYGVPF SRTEEGKIYQ
RPFGGMTTEY GKGKAAQRTC AAADRTGHAI LHTLYQQSLK HKVQFFVEYF AIDLLMEDGE
CRGVVAWNLD DGSLHCFRAH NVVLATGGYG RAYFSATSAH TCTGDGGGMA IRAGLPLQDM
EFVQFHPTGI YSAGCLITEG ARGEGGYLVN ANGERFMERY APAAKDLASR DVVSRAMTIE
IREGRGVGEH KDHVFLHLNH LSPEILHSRL PGISETAKIF AGVDVTKEPI PVLPTVHYNM
GGIPTNYHGQ VIIKDGKNHN SVVKGLMAIG EAACVSVHGA NRLGSNSLLD LVVFGRSSAL
KAAELIKPAS PHRSIKEESL EKIINRFDKV RHANGNILVA ELRLKMQRTM QSHASVFRTQ
EVLDEGAGMI SEIRSGYKDI KINDKSLIWN SDLVEALELD NLLDQALVTV YSAAARKESR
GAHAREDYPD RNDEDWMKHT LSSIDEAGKV VLDYKPVTLT TLTDEVTAVP PVKRVY
