ID A0A075R2T0_BRELA Unreviewed; 587 AA.
AC A0A075R2T0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=BRLA_c011730 {ECO:0000313|EMBL:AIG25513.1};
OS Brevibacillus laterosporus LMG 15441.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG25513.1, ECO:0000313|Proteomes:UP000005850};
RN [1] {ECO:0000313|EMBL:AIG25513.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG25513.1};
RX PubMed=21914864; DOI=10.1128/JB.05696-11;
RA Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT invertebrates.";
RL J. Bacteriol. 193:5535-5536(2011).
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:0000256|ARBA:ARBA00000030};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
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DR EMBL; CP007806; AIG25513.1; -; Genomic_DNA.
DR RefSeq; WP_003334940.1; NZ_CP007806.1.
DR AlphaFoldDB; A0A075R2T0; -.
DR STRING; 1042163.BRLA_c011730; -.
DR KEGG; blr:BRLA_c011730; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_7_1_9; -.
DR Proteomes; UP000005850; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 2.
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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AIG25513.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005850};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 6..392
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 452..579
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 465..492
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 587 AA; 65429 MW; AD78751C85CD14DB CRC64;
MAKGKLIIVG GGLAGLMATI KAAEKGVAVE LFSLVPVKRS HSVCAQGGIN GAVNTKGEGD
STWEHFDDTI YGGDFLANQP PVKAMCDAAP GIIYMLDRMG VMFNRTPEGL LDFRRFGGTK
HHRTAFAGAT TGQQLLYALD EQVRRYETEG LVKKYEYWDF LGAVLDDAGV CRGITAQSMR
SGEIKAFHAD AVIMATGGPG IIFGKSTNSI INTGTAASAL YQQGVIYANG EFIQIHPTAI
PGDDKLRLMS ESARGEGGRI WTYKDGKPWY FLEEKYPAYG NLVPRDIATR EIFHVCVDMK
LGINGENMVY LDLSHKDPKE LDVKLGGIIE IYEKFVGEDP RKVPMRIFPA VHYSMGGMWV
DYNQMTNIPG LFAAGECDYS QHGGNRLGAN SLLSAIYGGM VAGPNAINYI NSLDKLSDDL
PSSLFDSYSK QEQEKYDNIL KMDGTENAYV IHKELGEWMT DNVTVVRYND RLQKTDDKIL
ELMERYKNIN IQDTQQWSNS GAQFTRHLWN MLVLARAVTI SALQRDESRG AHYKPEFPER
DDERFMKTTM AKYNPETTAP EIYYEDIDVS LIKPRKRDYT SDKKGGK
//
