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Database: UniProt
Entry: I8J0W8_9BACI
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Original site: I8J0W8_9BACI 
ID   I8J0W8_9BACI            Unreviewed;       587 AA.
AC   I8J0W8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
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:EIT85401.1};
GN   ORFNames=A374_11675 {ECO:0000313|EMBL:EIT85401.1};
OS   Fictibacillus macauensis ZFHKF-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT85401.1, ECO:0000313|Proteomes:UP000004080};
RN   [1] {ECO:0000313|EMBL:EIT85401.1, ECO:0000313|Proteomes:UP000004080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT85401.1,
RC   ECO:0000313|Proteomes:UP000004080};
RX   PubMed=22887677; DOI=10.1128/JB.01049-12;
RA   Cai L., Zhang T.;
RT   "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming Bacterium.";
RL   J. Bacteriol. 194:4780-4780(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:EIT85401.1}.
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DR   EMBL; AKKV01000026; EIT85401.1; -; Genomic_DNA.
DR   RefSeq; WP_007202419.1; NZ_AKKV01000026.1.
DR   AlphaFoldDB; I8J0W8; -.
DR   STRING; 1196324.A374_11675; -.
DR   PATRIC; fig|1196324.3.peg.2392; -.
DR   eggNOG; COG1053; Bacteria.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000004080; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.820; -; 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   Reference proteome {ECO:0000313|Proteomes:UP000004080};
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;  64976 MW;  60D5A25C74A59D8F CRC64;
     MSKGNIIIVG GGLAGLMATI KAAEAGMKVD LFSLVPVKRS HSVCAQGGIN GAVNTKGEGD
     SPMVHFDDSV YGGDFLANQT PVKAMCEAAP GIIHLMDRMG VMFNRTPEGL LDFRRFGGTQ
     HHRTAFAGAT TGQQLLYALD EQVRRYEVAG LVTKYEGWEF LSAVVDDEGV CRGITSQNLK
     SMEIHSFKAD AVIMATGGPG IIFGKSTNSI INTGAAAASL YQQGVDYANG EFIQIHPTAI
     PGDDKLRLMS ESARGEGGRV WTYKDGKPWY FLEEKYPAYG NLVPRDIATR EIFSVCVDQK
     LGLNGENMVY LDLSHKDPKE LDIKLGGIIE IYEKFMGDDP RKVPMKIFPA VHYSMGGMWV
     DFNQMTNIPG LFAAGECEYQ YHGANRLGAN SLLSAIFGGM EAGPAAVSYV NGLAKSSEDL
     PSSVFEGQVR KEQEKYDNIM SLDGTENAYV LHKELGEWMT ANVTVVRYND KLQATDNKIQ
     ELMERYKKIN INDTSKWSNQ GASFTRQLWH MLQLGRVITL GALNRDESRG AHYKPDFPDR
     NDEDWLKTTR ASFNAATNGP DFSYEEVDIQ YIKPRKRDYS KKKEEVK
//
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