ID S0ARA0_FERAC Unreviewed; 564 AA.
AC S0ARA0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=FACI_IFERC00001G1743 {ECO:0000313|EMBL:AGO61723.1};
OS Ferroplasma acidarmanus Fer1.
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Ferroplasmaceae; Ferroplasma.
OX NCBI_TaxID=333146 {ECO:0000313|EMBL:AGO61723.1, ECO:0000313|Proteomes:UP000014660};
RN [1] {ECO:0000313|EMBL:AGO61723.1, ECO:0000313|Proteomes:UP000014660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=fer1 {ECO:0000313|Proteomes:UP000014660};
RX PubMed=17267615; DOI=10.1073/pnas.0604851104;
RA Allen E.E., Tyson G.W., Whitaker R.J., Detter J.C., Richardson P.M.,
RA Banfield J.F.;
RT "Genome dynamics in a natural archaeal population.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1883-1888(2007).
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; CP004145; AGO61723.1; -; Genomic_DNA.
DR RefSeq; WP_009887780.1; NC_021592.1.
DR AlphaFoldDB; S0ARA0; -.
DR GeneID; 16025932; -.
DR KEGG; fac:FACI_IFERC01G1743; -.
DR PATRIC; fig|333146.12.peg.1771; -.
DR HOGENOM; CLU_014312_6_2_2; -.
DR Proteomes; UP000014660; 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 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:UP000014660};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 7..386
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 440..564
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 564 AA; 62615 MW; 196DCAD639065179 CRC64;
MEKKEYDAVI LGGGLAGLMA ANMVAAGGFT VAVVSKVFPT RSHSSAAEGG IAAYIMGNSD
PNDDPDFMSY DEVKGGDYLV DQDAAELLSK KSGEIVNLLD AWGAPFNRQP DGRIALRYFG
GQTYPRTRFI ADKTGMALLH TLFEHSTGFK NIDFYNEYYV LDIAREGDSV NGLVAMEMKT
LDPIYLKSRA LLIASGGIGM MYKHSTNSYI NTGDGHGIAL RSGVALKDPE FVQFHPTGLY
PSDILISEAA RAEGAILKNN KGERFMARYA PHKFDLAPRD IVSRSMAIEI REGRGFEGGY
LGLDLRHLGK KYILERLTLA YDAAKNFSGV DAAEEMIPVR PAQHYFMGGI DVDITGTNHD
LKGVFAAGEA ACVSVHGANR LGSNSLLETL VYGRETGNAM VEYLKSHKKI ESNSDVDKLV
DNAYAYIKRE SGEHFGVLTE ELRDIMWDNV GIFRDNDKLA QAISKIKDLR TRSRSMYVTD
KSTNYNTELF NALETRNMID VAYAMATGAL NRTETRGAHF RDDFPERNDK DWMKHTITYL
AGDEIKISYK PVTYTRWKPE PRVY
//
