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Database: UniProt
Entry: K6CXU0_9BACI
LinkDB: K6CXU0_9BACI
Original site: K6CXU0_9BACI 
ID   K6CXU0_9BACI            Unreviewed;       583 AA.
AC   K6CXU0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE            EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN   Name=sdhA {ECO:0000313|EMBL:EKN65027.1};
GN   ORFNames=BABA_21731 {ECO:0000313|EMBL:EKN65027.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN65027.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN65027.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKN65027.1}.
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DR   EMBL; AJLS01000138; EKN65027.1; -; Genomic_DNA.
DR   RefSeq; WP_007087338.1; NZ_AJLS01000138.1.
DR   AlphaFoldDB; K6CXU0; -.
DR   STRING; 1117379.BABA_21731; -.
DR   PATRIC; fig|1117379.3.peg.4504; -.
DR   eggNOG; COG1053; Bacteria.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000006316; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:EKN65027.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006316};
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   583 AA;  64552 MW;  0B8C15EF31579C39 CRC64;
     MSKGKVIVVG GGLAGLMATI KVAETGTPVE LFSLVPVKRS HSVCAQGGIN GAVNTKGEGD
     SPWIHFDDTV YGGDFLANQP PVKAMCDAAP FIINLFDRMG VMFNRTPEGL LDFRRFGGTQ
     HHRTAFAGAT TGQQLLYALD EQVRRFEVDG LVTKYEGWEF LGAVVDDDGV CRGVVVQNLK
     TMEIKSFAAD AVIMATGGPG IIFGKSTNSV INTGSAASIV YQQGATYANG EMIQIHPTAI
     PGDDKLRLMS ESARGEGGRI WTYKDGKPWY FLEEKYPAYG NLVPRDIATR EIFDVCVRQK
     LGINGENMVF LDLSHKDPHE LDVKLGGIIE IYEKFMGDNP RKVPMKIFPA VHYSMGGLWV
     DYDQMTTIPG LFAAGECDYS QHGANRLGAN SLLSAVYGGM VAGPNAVNYV DGLEKTSEAV
     SSSVFDRHVK EQEEKWNGIM SLSGTENAYV LHKELGEWMT DNVTVVRYND QLLKTDEKIQ
     ELLERYQNIN INDTSKWSNQ GAAFTRQLQN MLQLARVITI GAYNRNESRG AHYKPDFPKR
     NDEEFLKTTM AKFVDAKTAP EFHYADVDTS LLKPRERDYT KKH
//
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