SDHA_RICTY
ID SDHA_RICTY Reviewed; 596 AA.
AC Q68XN9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Succinate dehydrogenase flavoprotein subunit;
DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P0AC41};
GN Name=sdhA; OrderedLocusNames=RT0117;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03603.1; -; Genomic_DNA.
DR RefSeq; WP_011190590.1; NC_006142.1.
DR AlphaFoldDB; Q68XN9; -.
DR SMR; Q68XN9; -.
DR STRING; 257363.RT0117; -.
DR EnsemblBacteria; AAU03603; AAU03603; RT0117.
DR KEGG; rty:RT0117; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_1_5; -.
DR OMA; DPIPIQP; -.
DR OrthoDB; 153138at2; -.
DR UniPathway; UPA00223; UER01005.
DR Proteomes; UP000000604; 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_0000280978"
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; 65743 MW; 5B4F534F1490ECE1 CRC64;
MTKAYNIIHH KFDVVVVGAG GAGLRSAFGM AKEGLNTACI TKIFPTRSHT VAAQGGISAA
LGNMGEDDWR WHMYDTVKGS DWLGDQDAIE YMCKNAPDAI LELEHYGVPF SRTEDGKIYQ
RPFGGMTTEY GKGKAAQRTC AAADRTGHAI LHTLYQQSLK HKVQFFIEYF AIDLLMEDGE
CRGVVAWNLD DGSLHCFRAH NVVLATGGYG RAYFSATSAH TCTGDGGGMV IRAGLPLQDM
EFVQFHPTGI YSAGCLITEG ARGEGGYLVN ANGERFMERY APAAKDLASR DVVSRAMTIE
IREGRGVGEY KDHVFLHLNH LSPEILHRRL PGISETAKIF AGVDVTKDPI PVLPTVHYNM
GGIPTNYHGQ VIIKDGKNHN SIVNGIMAIG EAACVSVHGA NRLGSNSLLD LVVFGRSSAL
KAAELIKPVS PHKPLKKEIL EKIINRFDKI RHANGNVLVA DLRLQMQRTM QSHVSVFRTQ
ELLDEGARMI SEIRNRYKDI KINDKSLIWN SDLVEALELD NLLDQALVTV YSAAARKESR
GAHAREDYPD RNDIDWIKHT LSSIDDSGQI ILDYKPVTLT TLTDEISTIP PVKRIY
