ID A0A1G5HRS6_9BACL Unreviewed; 580 AA.
AC A0A1G5HRS6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=SAMN05720606_107164 {ECO:0000313|EMBL:SCY66434.1};
OS Paenibacillus polysaccharolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=582692 {ECO:0000313|EMBL:SCY66434.1, ECO:0000313|Proteomes:UP000198538};
RN [1] {ECO:0000313|EMBL:SCY66434.1, ECO:0000313|Proteomes:UP000198538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL9 {ECO:0000313|EMBL:SCY66434.1,
RC ECO:0000313|Proteomes:UP000198538};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FMVM01000007; SCY66434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5HRS6; -.
DR STRING; 582692.SAMN05720606_107164; -.
DR Proteomes; UP000198538; 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 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 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..577
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 580 AA; 63968 MW; 87CD28F7C2BC1E28 CRC64;
MASSNVIIVG GGLAGLMAAI KSAEAGVHVH LFSLVPVKRS HSVCAQGGIN GAVNTKGEGD
SPWVHFDDTV YGGDFLANQP PVKAMCEAAP GIIHLMDRMG VMFNRTPEGL LDFRRFGGTK
HHRTAFAGAT TGQQLLYALD EQVRRWEAAG LVTKYENWEF LQAVVDDEGV CRGIVAQDLK
TMKVQTFPAE AVILASGGPG IIFGKTTNSV INTGTAASAV YQQGVNYANG EFIQIHPTAI
PGDDKLRLMS ESARGEGGRI WTYKDGKPWY FLEEKYPSYG NLVPRDIATR EIFSVCVDMG
LGVNGENMVY LDLSHKDPKE LDVKLGGIIE IYEKFMGDDP RKIPMKIFPA VHYSMGGMWV
DYNQMTNIPG LFAAGECEYQ YHGANRLGAN SLVSAIYGGM VAGPKAAEYI KGLKKSSADI
SSSVFDGYTK RQTDKYEGIM KMQGTENAYV IHKELGEWMT ANMTVVRYND KLEATIGKIK
ELKERYGKIN MYDNSGWNNP GAAFTRQLWN MLELSEAMTL GALLRNESRG AHYKPEFTER
NDEEFLKTTI ASWSKEGPQI SYEPVDVSLI PPRIRDYSKD
//
