ID A0A2T6BTC0_9BACL Unreviewed; 591 AA.
AC A0A2T6BTC0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=C8P63_11230 {ECO:0000313|EMBL:PTX59335.1};
OS Melghirimyces profundicolus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Melghirimyces.
OX NCBI_TaxID=1242148 {ECO:0000313|EMBL:PTX59335.1, ECO:0000313|Proteomes:UP000244240};
RN [1] {ECO:0000313|EMBL:PTX59335.1, ECO:0000313|Proteomes:UP000244240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45787 {ECO:0000313|EMBL:PTX59335.1,
RC ECO:0000313|Proteomes:UP000244240};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-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:PTX59335.1}.
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DR EMBL; QBKR01000012; PTX59335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6BTC0; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000244240; 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:UP000244240};
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 591 AA; 66357 MW; 4D7DEE796036A6AB CRC64;
MKKEKVIIVG GGLAGLMATV KVAEAGADVD LFSIVPVRRS HSVCAQGGIN GAVNTKGEGD
SPWEHFDDTI YGGDFLANQP PVKAMTEAAP GIIYLMDRMG VPFNRTPEGL LDFRRFGGTR
HHRTAFAGAT TGQQLLYALD EQVRRWEVAG NVTKYEHWEF LSIVQDDEGR CRGIVAQDRR
SMEIRAFRAD AVIMASGGPG IIFGKSTNSM INTGTAASAV YQQGAYYANG EFIQVHPTAI
PGDDKLRLMS ESARGEGGRV WTYKDGKPWY FLEEMYPAYG NLVPRDIATR AIFKVCVDMK
LGINGENMVY LDLSHKDPKE LDIKLGGIIE IYEKFMGEDP RKVPMKIFPA VHYSMGGLWV
DFNQMTNIPG LFAAGECEYQ YHGANRLGAN SLLSCIFGGM VAGPNALEYI RGLDKSAEDL
SSTLFEAQQK KEQEKYDNIL KMDGDENPYK LHKELGEWMT DNVTVVRYND RLKKTDDKIQ
ELMERWKRIN VGDTSTWSNQ SASFVRQLWN MLELARVITL GAYNRNESRG AHYKPEFPER
NDEEWLKTTK AKYTENGPAF EYEEVDTSLI KPRPRRYDVA KQAEEKGAES Q
//
