ID A0A0Q3W0F3_9BACI Unreviewed; 586 AA.
AC A0A0Q3W0F3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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:KQL34083.1};
GN ORFNames=AN959_13730 {ECO:0000313|EMBL:KQL34083.1};
OS Psychrobacillus sp. FJAT-21963.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=1712028 {ECO:0000313|EMBL:KQL34083.1, ECO:0000313|Proteomes:UP000051878};
RN [1] {ECO:0000313|EMBL:KQL34083.1, ECO:0000313|Proteomes:UP000051878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-21963 {ECO:0000313|EMBL:KQL34083.1,
RC ECO:0000313|Proteomes:UP000051878};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) 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:KQL34083.1}.
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DR EMBL; LJIY01000006; KQL34083.1; -; Genomic_DNA.
DR RefSeq; WP_056831487.1; NZ_LJIY01000006.1.
DR AlphaFoldDB; A0A0Q3W0F3; -.
DR PATRIC; fig|1712028.3.peg.1353; -.
DR Proteomes; UP000051878; 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; 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:UP000051878};
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 586 AA; 64836 MW; 2111E0634C25DAE0 CRC64;
MAKSKLIVVG GGLAGLMATM KAAEDGTHVD LFSLVPVKRS HSVCAQGGIN GAVNTKGEGD
SPAVHLDDTV YGGDFLANQG PVKAMTDAAP GIINLFDRMG VMFNRTPEGL LDFRRFGGTL
MHRTAFAGAT TGQQLLYALD EQVRRFEVDG LVTKFEGWEF LGIIKDSEGV CRGIKAQNLK
TMEIRAFRGD AVIMATGGPG IIFGKTTNSI INTGSAASIV YQQGAYYSNG EFIQIHPTAI
PGDDKLRLMS ESARGEGGRI WTYKDGKPWY FLEEKYPAYG NLVPRDIATR EIFDVCVNQK
LGINGENMVY LDLSHKDPHE LDVKLGGIIE IYEKFTGDDP RKVPMKIFPA VHYSMGGLWV
DEDQMTNIPG LFAAGECDYS QHGANRLGAN SLLSAVFGGS VAGPNAVKYM RNLDSHAEDM
DSTIFDAEVQ LEQEKWDKTL AMKGTENAYL LHKELGEWMT DNVTVVRYND KLEATDKKIQ
ELLERYENIN MDDTQKWSNQ GASFTRQLKN MLYLARVITI GALKRNESRG AHYKPDFPER
NDEEFLKTTM AKFDPATGAP VIYYEEVDVS LVPPRKRDYS STKGEK
//
