ID F3KKX5_9ARCH Unreviewed; 570 AA.
AC F3KKX5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=Nlim_1209 {ECO:0000313|EMBL:EGG41976.1};
OS Candidatus Nitrosarchaeum limnium SFB1.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosarchaeum.
OX NCBI_TaxID=886738 {ECO:0000313|EMBL:EGG41976.1};
RN [1] {ECO:0000313|EMBL:EGG41976.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB1 {ECO:0000313|EMBL:EGG41976.1};
RX PubMed=21364937; DOI=10.1371/journal.pone.0016626;
RA Blainey P.C., Mosier A.C., Potanina A., Francis C.A., Quake S.R.;
RT "Genome of a low-salinity ammonia-oxidizing archaeon determined by single-
RT cell and metagenomic analysis.";
RL PLoS ONE 6:E16626-E16626(2011).
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:EGG41976.1}.
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DR EMBL; AEGP01000043; EGG41976.1; -; Genomic_DNA.
DR AlphaFoldDB; F3KKX5; -.
DR STRING; 886738.Nlim_1209; -.
DR PATRIC; fig|886738.10.peg.1327; -.
DR HOGENOM; CLU_014312_6_2_2; -.
DR Proteomes; UP000004348; Chromosome.
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 Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 8..389
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 447..570
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 570 AA; 63849 MW; C6721996CF6E04BD CRC64;
MVESLEFDLI ICGSGLAGLR AAIEAARKNP KIKIGIVSKV QVMRSHSVSA EGGTAAVLFE
DEGDTIESHI YDTVKGSDFL ADQDVAERLC VEMPKEIYQL DHWGMPWSRR KDGRIGQRNF
GGYSFPRATY ASDKVGFFEM QTLYDTCQKH ENIEYLNEWF ATSIIHDGKR FLGITAIELS
SGTFYSIKGK ALIIATGGAG RLYSFSTYAL SSTPDGLDMA LRAGMALKDM EFVQFHPTGI
LPSGILITEG ARGEGGYLLN NKGERFMKKY AGEKMELAPR DIVSRAMMTE MSEGRGFKHE
TGVDCMKLDL RHLGDEKIKE KLGGIREISI KFSGLDPATE VLDVRPVCHY MMGGIHTDID
GATELQGVWA AGEAACNSVH GSNRLGANST SECIVWGKIT GNLAVDYIEK FDMATHWPHH
LVAAEEKRIY DGIFRGNGDV NPYEVKQELT DTMNDKAYVF RNEKNLVEGL KKIRQLKQQA
WKHVDDKAKE YNTNFSNVME LDSMFRVAEI VLLGAINRKE SRGAHSRTDY PKRDDANFLH
HTLAYYDPKE PIMKTHPVTI TKYQPVERKY
//
