ID   DHSA_RICPR              Reviewed;         596 AA.
AC   P31038;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-NOV-2008, entry version 74.
DE   RecName: Full=Succinate dehydrogenase flavoprotein subunit;
DE            EC=1.3.99.1;
GN   Name=sdhA; OrderedLocusNames=RP128;
OS   Rickettsia prowazekii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=782;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   MEDLINE=94040788; 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
RT   encoding 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   MEDLINE=99039499; PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O.,
RA   Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K.,
RA   Eriksson A.-S., Winkler H.H., 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: Succinate + acceptor = fumarate + reduced
CC       acceptor.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC       flavoprotein, an iron-sulfur, cytochrome b-556, and an hydrophobic
CC       anchor protein.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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; -.
DR   HSSP; P10444; 1NEK.
DR   GeneID; 883752; -.
DR   GenomeReviews; AJ235269_GR; RP128.
DR   KEGG; rpr:RP128; -.
DR   HOGENOM; P31038; -.
DR   BioCyc; RPRO272947:RP128-MON; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; IEA:EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR003953; FAD_bind2_N.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR003952; FRD_SDH_FAD_BS.
DR   InterPro; IPR004112; Fum_Rdtase/Succ_DHase_flav_C.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR011281; Succ_DHase_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_frdA_Gneg.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
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; Complete proteome;
KW   Electron transport; FAD; Flavoprotein; Membrane; Oxidoreductase;
KW   Transport; Tricarboxylic acid cycle.
FT   CHAIN         1    596       Succinate dehydrogenase flavoprotein
FT                                subunit.
FT                                /FTId=PRO_0000158657.
FT   NP_BIND      41     56       FAD (By similarity).
FT   ACT_SITE    290    290       Proton acceptor (By similarity).
FT   BINDING     246    246       Substrate (By similarity).
FT   BINDING     258    258       Substrate (By similarity).
FT   BINDING     357    357       Substrate (By similarity).
FT   BINDING     402    402       Substrate (By similarity).
FT   MOD_RES      49     49       Tele-8alpha-FAD histidine (By
FT                                similarity).
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
//