SDHA_BACSU
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 03-AUG-2022, entry version 167.
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; Firmicutes; 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; P08065; -.
DR PRIDE; P08065; -.
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 OMA; DPIPIQP; -.
DR PhylomeDB; P08065; -.
DR BioCyc; BSUB:BSU28440-MON; -.
DR BioCyc; MetaCyc:BSU28440-MON; -.
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: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; 3.50.50.60; -; 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; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR PANTHER; PTHR11632:SF53; PTHR11632:SF53; 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; TIGR01811; sdhA_Bsu; 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
