ID A0A1I0K5W7_9BACL Unreviewed; 579 AA.
AC A0A1I0K5W7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN03159358_3863 {ECO:0000313|EMBL:SEU19201.1};
OS Paenibacillus sp. NFR01.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566279 {ECO:0000313|EMBL:SEU19201.1, ECO:0000313|Proteomes:UP000198735};
RN [1] {ECO:0000313|EMBL:SEU19201.1, ECO:0000313|Proteomes:UP000198735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NFR01 {ECO:0000313|EMBL:SEU19201.1,
RC ECO:0000313|Proteomes:UP000198735};
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; FOIK01000004; SEU19201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0K5W7; -.
DR STRING; 1566279.SAMN03159358_3863; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000198735; 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 Reference proteome {ECO:0000313|Proteomes:UP000198735};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..391
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 451..576
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 284
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 579 AA; 64075 MW; 879388C13D2B1127 CRC64;
MASDIIIVGG GLAGLMATIK AAESGAHVHL FSLVPVKRSH SVCAQGGING AVNTKGEGDS
PWEHFDDTVY GGDFLANQPP VKAMCEAAPG IIHLMDRMGV MFNRTPEGLL DFRRFGGTKR
HRTAFAGATT GQQLLYALDE QVRRWETEGL VTKSENWEFL SVILDDDGVC RGISAQNLKT
MEIETFPADA VILASGGPGI IFGKTTNSVI NTGTAASAVY QQGVHYANGE FIQIHPTAIP
GDDKLRLMSE SARGEGGRIW TYKDGKPWYF LEEKYPSYGN LVPRDIATRE IFNVCVDQGL
GINGENMVYL DLSHKDPKEL DVKLGGIIEI YEKFMGDDPR KIPMKIFPAV HYSMGGLWVD
YNQMTNIPGL FAAGECEYQY HGANRLGANS LVSAIYGGMM AGPKAVEYIK GLKKSVQDVS
STVFDRFHKK QTDKYEALLN MSGTENAYVI HKELGEIMTA NMTVVRDNKR LSETIGKIKD
FKERYRNINM SDTSRWNNQG VAFTRQLGNM LELAEAMTLG ALLRNESRGA HYKPEFPNRN
DEEFLKTTKA TWTADGPQIS YEDVDVSLIP PRVRDYSKD
//
