ID A0A2U3ANL8_9BACL Unreviewed; 583 AA.
AC A0A2U3ANL8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=DEX24_04200 {ECO:0000313|EMBL:PWI26133.1};
OS Kurthia sibirica.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=202750 {ECO:0000313|EMBL:PWI26133.1, ECO:0000313|Proteomes:UP000245938};
RN [1] {ECO:0000313|EMBL:PWI26133.1, ECO:0000313|Proteomes:UP000245938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49154 {ECO:0000313|EMBL:PWI26133.1,
RC ECO:0000313|Proteomes:UP000245938};
RA Maclea K.S., Goen A.E.;
RT "Kurthia sibirica genome sequence.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:PWI26133.1}.
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DR EMBL; QFVR01000004; PWI26133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3ANL8; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000245938; 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 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:UP000245938};
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..578
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 583 AA; 64441 MW; 16EAC0D6B0C269D4 CRC64;
MAKSKLIVVG GGLAGLMSSM KAAELGTEVE LFSLVPVKRS HSVCAQGGIN GAVNTKGEGD
SPWIHFDDTV YGGDFLANQP PVKAMCDAAP GIIHLFDRMG VMFNRTPEGL LDFRRFGGTM
HHRTAFAGAT TGQQLLYALD EQVRKWEVEG LVTKYEGWEF LGLVLDENGV CKGIKAQDLT
THEIKAFPAD AVIMASGGPG IIFGKSTNSM INTGSAASIV YQQGAKYANG EFIQIHPTAI
PGDDKLRLMS ESARGEGGRI WTYKDGKPWY FLEEKYPAYG NLVPRDVATR EIFDVCINQK
LGVNGENVVY LDLSHKDPHE LDIKLGGIIE IYQKFVGDDP HKVPMKIFPA VHYSMGGLWV
DYDQQTTIPG AFAAGECDYS QHGGNRLGAN SLLSAIYGGS VAGPNAVNYI KHLDTHVEDL
PTAIYEDAVK EEQAKWDEVM SLKGTENAYL LHKELGEVMT NNVTVVRHND RLENTLVKLE
ELKERWNNID INDTNKWSNQ GVQFTRQLKN MIALAFVITK GALLRDESRG AHYKPDFPER
NDEDFLKTTI AQFTPSFDPI ITYEEVDVSM IKPRKRDYTG GAH
//