ID   SDHA_BACSU              Reviewed;         586 AA.
AC   P08065;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 4.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Succinate dehydrogenase flavoprotein subunit;
DE            EC=1.3.5.1 {ECO:0000250|UniProtKB:P0AC41};
GN   Name=sdhA; Synonyms=citF; OrderedLocusNames=BSU28440;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / PY79;
RX   PubMed=3027051; DOI=10.1128/jb.169.2.864-873.1987;
RA   Phillips M.K., Hederstedt L., Hasnain S., Rutberg L., Guest J.R.;
RT   "Nucleotide sequence encoding the flavoprotein and iron-sulfur protein
RT   subunits of the Bacillus subtilis PY79 succinate dehydrogenase complex.";
RL   J. Bacteriol. 169:864-873(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 82; 100; 390 AND 441.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RC   STRAIN=168 / PY79;
RX   PubMed=3086287; DOI=10.1128/jb.166.3.1067-1071.1986;
RA   Magnusson K., Philips M.K., Guest J.R., Rutberg L.;
RT   "Nucleotide sequence of the gene for cytochrome b558 of the Bacillus
RT   subtilis succinate dehydrogenase complex.";
RL   J. Bacteriol. 166:1067-1071(1986).
RN   [6]
RP   MUTANT ASP-48.
RX   PubMed=3021212; DOI=10.1021/bi00366a033;
RA   Maguire J.J., Magnusson K., Hederstedt L.;
RT   "Bacillus subtilis mutant succinate dehydrogenase lacking covalently bound
RT   flavin: identification of the primary defect and studies on the iron-sulfur
RT   clusters in mutated and wild-type enzyme.";
RL   Biochemistry 25:5202-5208(1986).
RN   [7]
RP   INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=23651456; DOI=10.1111/mmi.12252;
RA   Bach J.N., Bramkamp M.;
RT   "Flotillins functionally organize the bacterial membrane.";
RL   Mol. Microbiol. 88:1205-1217(2013).
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: In B.subtilis succinate dehydrogenase forms part of an enzyme
CC       complex containing three subunits: a flavoprotein, an iron-sulfur
CC       protein and cytochrome b-558. Interacts with FloT (PubMed:23651456).
CC       {ECO:0000269|PubMed:23651456}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P0AC41,
CC       ECO:0000269|PubMed:23651456}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P0AC41}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P0AC41}. Membrane raft
CC       {ECO:0000269|PubMed:23651456}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P0AC41}. Note=Present in detergent-resistant
CC       membrane (DRM) fractions that may be equivalent to eukaryotic membrane
CC       rafts; these rafts include proteins involved in signaling, molecule
CC       trafficking and protein secretion. {ECO:0000269|PubMed:23651456}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
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DR   EMBL; M13470; AAA22746.1; -; Genomic_DNA.
DR   EMBL; Z75208; CAA99547.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14804.2; -; Genomic_DNA.
DR   PIR; A27763; A27763.
DR   RefSeq; NP_390722.2; NC_000964.3.
DR   RefSeq; WP_003229567.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P08065; -.
DR   SMR; P08065; -.
DR   IntAct; P08065; 1.
DR   MINT; P08065; -.
DR   STRING; 224308.BSU28440; -.
DR   jPOST; P08065; -.
DR   PaxDb; 224308-BSU28440; -.
DR   EnsemblBacteria; CAB14804; CAB14804; BSU_28440.
DR   GeneID; 937600; -.
DR   KEGG; bsu:BSU28440; -.
DR   PATRIC; fig|224308.179.peg.3089; -.
DR   eggNOG; COG1053; Bacteria.
DR   InParanoid; P08065; -.
DR   OrthoDB; 9806724at2; -.
DR   PhylomeDB; P08065; -.
DR   BioCyc; BSUB:BSU28440-MONOMER; -.
DR   BioCyc; MetaCyc:BSU28440-MONOMER; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; 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:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.10.20.820; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 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; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   NCBIfam; TIGR01811; sdhA_Bsu; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF53; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Electron transport; FAD; Flavoprotein; Membrane;
KW   Oxidoreductase; Reference proteome; Transport; Tricarboxylic acid cycle.
FT   CHAIN           1..586
FT                   /note="Succinate dehydrogenase flavoprotein subunit"
FT                   /id="PRO_0000158650"
FT   ACT_SITE        285
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         33..48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         376
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         386
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   BINDING         391..392
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   MOD_RES         41
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   VARIANT         48
FT                   /note="G -> D (in a defective mutant)"
FT   CONFLICT        82
FT                   /note="V -> L (in Ref. 1; AAA22746 and 2; CAA99547)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="G -> A (in Ref. 1; AAA22746 and 2; CAA99547)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        388..390
FT                   /note="GAN -> ERT (in Ref. 1; AAA22746 and 2; CAA99547)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        441
FT                   /note="S -> I (in Ref. 1; AAA22746 and 2; CAA99547)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   586 AA;  65152 MW;  F2327C2B383DE671 CRC64;
     MSQSSIIVVG GGLAGLMATI KAAESGMAVK LFSIVPVKRS HSVCAQGGIN GAVNTKGEGD
     SPWEHFDDTV YGGDFLANQP PVKAMCEAAP SIIHLLDRMG VMFNRTPEGL LDFRRFGGTQ
     HHRTAYAGAT TGQQLLYALD EQVRRYEVAG LVTKYEGWEF LGAVLDDDRT CRGIVAQNLT
     NMQIESFRSD AVIMATGGPG IIFGKSTNSM INTGSAASIV YQQGAYYANG EFIQIHPTAI
     PGDDKLRLMS ESARGEGGRV WTYKDGKPWY FLEEKYPAYG NLVPRDIATR EIFDVCVNQK
     LGINGENMVY LDLSHKDPKE LDIKLGGIIE IYEKFMGDDP RKLPMKIFPA VHYSMGGLWV
     DYDQMTNIPG LFAAGECDYS MHGGNRLGAN SLLSAIYGGM VAGPNAVKYV NGLESSAEDM
     SSSLFDAHVK KEEEKWADIM SMDGTENAYV LHKELGEWMT ANVTVVRHND KLLKTDDKIQ
     ELMERFKKIN INDTTKWSNQ GAMFTRQFSN MLQLARVITL GAYNRNESRG AHYKPDYPER
     NDDEWLKTTM AKHVSPYEAP EFEYQDVDVS LITPRKRDYS KKKVAK
//