ID Q6L0C2_PICTO Unreviewed; 560 AA.
AC Q6L0C2; A0A8G2FX98;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN OrderedLocusNames=PTO0995 {ECO:0000313|EMBL:AAT43580.1};
GN ORFNames=SAMN02745355_1127 {ECO:0000313|EMBL:SMD31204.1};
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828 / KAW 2/3).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=1122961 {ECO:0000313|EMBL:AAT43580.1, ECO:0000313|Proteomes:UP000000438};
RN [1] {ECO:0000313|EMBL:AAT43580.1, ECO:0000313|Proteomes:UP000000438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
RC {ECO:0000313|Proteomes:UP000000438}, and DSM 9790
RC {ECO:0000313|EMBL:AAT43580.1};
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Futterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
RN [2] {ECO:0000313|EMBL:AAT43580.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 9790 {ECO:0000313|EMBL:AAT43580.1};
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SMD31204.1, ECO:0000313|Proteomes:UP000192315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9789 {ECO:0000313|EMBL:SMD31204.1,
RC ECO:0000313|Proteomes:UP000192315};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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; AE017261; AAT43580.1; -; Genomic_DNA.
DR EMBL; FWYE01000003; SMD31204.1; -; Genomic_DNA.
DR RefSeq; WP_011177796.1; NZ_FWYE01000003.1.
DR AlphaFoldDB; Q6L0C2; -.
DR STRING; 263820.PTO0995; -.
DR PaxDb; 263820-PTO0995; -.
DR GeneID; 2844430; -.
DR KEGG; pto:PTO0995; -.
DR PATRIC; fig|263820.9.peg.1034; -.
DR eggNOG; arCOG00571; Archaea.
DR HOGENOM; CLU_014312_6_2_2; -.
DR InParanoid; Q6L0C2; -.
DR OrthoDB; 23539at2157; -.
DR Proteomes; UP000000438; Chromosome.
DR Proteomes; UP000192315; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
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; 4.10.80.40; succinate dehydrogenase protein 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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR PRINTS; PR00368; FADPNR.
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 ECO:0000313|EMBL:AAT43580.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192315};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 7..383
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 436..560
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 560 AA; 62349 MW; 65566B7EC4111BAB CRC64;
MEKMKYDAVI MGAGLAGLMA ANEIASAGYS VAVVSKVFPT RSHSSAAEGG IAAYIPGNSD
PNDDPDYMSY DEIKGGDYLV DQDAAELLSS KSGEIVRTLD SWGAPFNRQP DGRIALRYFG
GQTYPRTRFV GDKTGMALLH TLYERASGFN IDFYNEWYVI DLLKEKKAAG LVALKMRSLE
PIYLTAKAII IASGGLGMIY KHSTNSYINT GDGYGIALRA GVPLKDPEFV QFHPTGLYPS
DILISEAARA EGGILRNNKN ERFMEKYAPH KFDLAPRDIV SRSMTIEINE GRGFPGGYLG
LDLTHLGRDY IIERLSLAYE AAKTFAGVDA TEEMIPVRPA QHYFMGGIDV DITGASPLPG
LFAAGEAACV SVHGANRLGS NSLLETLVYG RETGKNVVEF LKKEHDIPDL NPEKSLDDAY
KYVKRETGEH FGSILNDLRE TMWDNVGIFR DEKKLSKAVS DIKSLRKRAE SLYVTDKSNN
YNTEFFNALE LRNMLDVAYV IAESALNRKE SRGAHYRTDF PDRNDDSWLK HTISYLSNED
VRIDYKPVKM TRWKPEVRVY
//
