SDHA_RICPR
ID SDHA_RICPR Reviewed; 596 AA.
AC P31038;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Succinate dehydrogenase flavoprotein subunit;
DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P0AC41};
GN Name=sdhA; OrderedLocusNames=RP128;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=8224887; DOI=10.1016/0378-1119(93)90238-x;
RA Aliabadi Z., Winkler H.H., Wood D.O.;
RT "Isolation and characterization of the Rickettsia prowazekii gene encoding
RT the flavoprotein subunit of succinate dehydrogenase.";
RL Gene 133:135-140(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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; M88696; AAA16097.1; -; Unassigned_DNA.
DR EMBL; U02603; AAA18327.1; -; Unassigned_DNA.
DR EMBL; AJ235270; CAA14597.1; -; Genomic_DNA.
DR PIR; JN0895; JN0895.
DR RefSeq; NP_220520.1; NC_000963.1.
DR RefSeq; WP_004597170.1; NC_000963.1.
DR AlphaFoldDB; P31038; -.
DR SMR; P31038; -.
DR STRING; 272947.RP128; -.
DR EnsemblBacteria; CAA14597; CAA14597; CAA14597.
DR GeneID; 57569256; -.
DR KEGG; rpr:RP128; -.
DR PATRIC; fig|272947.5.peg.130; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_1_5; -.
DR OMA; DPIPIQP; -.
DR UniPathway; UPA00223; UER01005.
DR Proteomes; UP000002480; 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; Reference proteome; Transport;
KW Tricarboxylic acid cycle.
FT CHAIN 1..596
FT /note="Succinate dehydrogenase flavoprotein subunit"
FT /id="PRO_0000158657"
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; 65445 MW; E5CAA5DFE9426EC4 CRC64;
MTKAYNIIHH KFDVVVVGAG GAGLRSAFGM AKEGLNTACI TKIFPTRSHT VAAQGGISAA
LGNMGEDDWR WHMYDTVKGS DWLGDQDAIE YMCKNAPDAI LELEHYGVPF SRTVDGKIYQ
RPFGGMTTEY GKGKAAQRTC AAADRTGHAI LHTLYQQSLK HKVQFFIEYF AIDLLMEDGE
CRGVVAWNLD DGSLHCFRAH NVVLATGGYG RAYFSATSAH TCTGDGGGMV IRAGLPLQDM
EFVQFHPTGI YSAGCLITEG ARGEGGYLVN ANGERFMERY APAAKDLASR DVVSRAMTIE
IREGRGVGEH KDHVFLHLNH LSPEILHRRL PGISETAKIF AGVDVTKDPI PVLPTVHYNM
GGIPTNYQGQ VIIKDGKNHN SIVNGIMAIG EAACVSVHGA NRLGSNSLLD LVVFGRSSAL
KAAELIKPAS PHKPLQKETL EKIINRFDKV RYANGNILVA DLRLKMQRTM QSHVSVFRTQ
KLLDEGVGMI SEIRNRYKDI KINDKSLIWN SDLVEALELD NLLDQALVTV CSAAARKESR
GAHAREDYPD RNDRDWIKHT LSSIDDSGKV VLDYKPVTLT TLTDAISAIP PVKRVY
