ID A0A089LUY0_9BACL Unreviewed; 581 AA.
AC A0A089LUY0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:AIQ65341.1};
GN ORFNames=PSTEL_21675 {ECO:0000313|EMBL:AIQ65341.1};
OS Paenibacillus stellifer.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ65341.1, ECO:0000313|Proteomes:UP000029507};
RN [1] {ECO:0000313|EMBL:AIQ65341.1, ECO:0000313|Proteomes:UP000029507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ65341.1,
RC ECO:0000313|Proteomes:UP000029507};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009286; AIQ65341.1; -; Genomic_DNA.
DR RefSeq; WP_038698315.1; NZ_CP009286.1.
DR AlphaFoldDB; A0A089LUY0; -.
DR STRING; 169760.PSTEL_21675; -.
DR KEGG; pste:PSTEL_21675; -.
DR HOGENOM; CLU_014312_7_1_9; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000029507; Chromosome.
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:UP000029507};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..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 581 AA; 64323 MW; 8BE6CDEB98500825 CRC64;
MATADIIIVG GGLAGLMATI KAAEAGVHVH LFSLVPVKRS HSVCAQGGIN GAVNTKGEGD
SPWVHFDDTV YGGDFLANQP PVKAMCEAAP GIIHLMDRMG VMFNRTPEGL LDFRRFGGTK
HHRTAFAGAT TGQQLLYALD EQVRRWEVEG FVTKRENWEF LSVVLDDEGV CRGICAQDLR
SMAIETFPAD AVILATGGPG IIFGKTTNSV INTGTAASAV YQQGVHYANG EFIQIHPTAI
PGDDKLRLMS ESARGEGGRI WTYKDGKPWY FLEEKYPAYG NLVPRDIATR EIFNVCVDQG
LGINGENMVY LDLSHKDPKE LDVKLGGIIE IYEKFMGDDP RKIPMKIFPA VHYSMGGMWV
DYNQMTNIPG LFAAGECEYQ YHGANRLGAN SLVSAIFGGM VSGPKAVEYI KGLKRSAQDV
SSSVFDSASR AQQDKYDNLL KMTGTENAYV IHKELGEWMT ANMTVVRHNP KLEATIGKIR
ELKERYRQIN MNDTSRWNNQ GAAFTRQLWN MLELAEAMTK GALLRNESRG AHYKPEFPSR
NDEEFLKTTK AAWTPDGPQI TYEDVDVSLI PPRVRDYSKD K
//
