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Database: UniProt
Entry: K0IIW2_NITGG
LinkDB: K0IIW2_NITGG
Original site: K0IIW2_NITGG 
ID   K0IIW2_NITGG            Unreviewed;       567 AA.
AC   K0IIW2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
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:AFU59028.1};
GN   OrderedLocusNames=Ngar_c20970 {ECO:0000313|EMBL:AFU59028.1};
OS   Nitrososphaera gargensis (strain Ga9.2).
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Nitrososphaerales;
OC   Nitrososphaeraceae; Nitrososphaera.
OX   NCBI_TaxID=1237085 {ECO:0000313|EMBL:AFU59028.1, ECO:0000313|Proteomes:UP000008037};
RN   [1] {ECO:0000313|EMBL:AFU59028.1, ECO:0000313|Proteomes:UP000008037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ga9.2 {ECO:0000313|Proteomes:UP000008037};
RX   PubMed=23057602; DOI=10.1111/j.1462-2920.2012.02893.x;
RA   Spang A., Poehlein A., Offre P., Zumbragel S., Haider S., Rychlik N.,
RA   Nowka B., Schmeisser C., Lebedeva E.V., Rattei T., Bohm C., Schmid M.,
RA   Galushko A., Hatzenpichler R., Weinmaier T., Daniel R., Schleper C.,
RA   Spieck E., Streit W., Wagner M.;
RT   "The genome of the ammonia-oxidizing Candidatus Nitrososphaera gargensis:
RT   insights into metabolic versatility and environmental adaptations.";
RL   Environ. Microbiol. 14:3122-45(2012).
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; CP002408; AFU59028.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0IIW2; -.
DR   STRING; 1237085.Ngar_c20970; -.
DR   KEGG; nga:Ngar_c20970; -.
DR   PATRIC; fig|1237085.11.peg.2077; -.
DR   HOGENOM; CLU_014312_6_2_2; -.
DR   InParanoid; K0IIW2; -.
DR   Proteomes; UP000008037; 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   ECO:0000313|EMBL:AFU59028.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008037};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          5..386
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          442..567
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   567 AA;  63261 MW;  3D9F449C118CDDB8 CRC64;
     MISHDVLIIG SGLAGLRAAI SAAAIDKKLS IAVISKVQVM RSHSVSAEGG TAAVLYEEEG
     DNQESHIYDT IKGSDFLADQ DVAERLVQNM PYEIYQMDHW GMPWSRRKDG RIAQRKFGGY
     SFPRATFAQD KVGFYLMQTL YDTCQKYDNI HFYNEWFCTS ILHENNTFQG ITAIELKTGN
     FTVFKAPAGI ICTGGAGRIY SFSTYAYSST PDGLDMAYRA GLALKDMEFV QFHPTGILPS
     GILITEGARG EGGYLINSNG ERFMQKYAPG KLELAPRDVV SRSMIKEIQE GRGFKHETGV
     DCLKLDLTHL GAERIKEVLA GIREIGIKFS GIDIIDEPIE VRPVCHYMMG GIHANVDGAT
     EMVGLWAAGE AACNSTHGAN RLGANSTSEC IVWGRITGEL AAKHAQERKA GSVQEQQVLD
     EEKRIYDGIF RGRGDVNPYE VRKQLTDTMD AKAYVFRNEQ GLTEALKKTR ELKAAMWKHV
     DDKAKEYNTN FVNVMEIDSM LRTAEVVLVG ALNRRESRGA HARTDYPYRD DANFLKHTLA
     YFTGNGGPKM TWYPVTFTRY APVERKY
//
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