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Database: UniProt
Entry: F6FPV4_ISOV2
LinkDB: F6FPV4_ISOV2
Original site: F6FPV4_ISOV2 
ID   F6FPV4_ISOV2            Unreviewed;       611 AA.
AC   F6FPV4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000256|ARBA:ARBA00019965, ECO:0000256|RuleBase:RU362051};
DE            EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU362051};
GN   OrderedLocusNames=Isova_0959 {ECO:0000313|EMBL:AEG43743.1};
OS   Isoptericola variabilis (strain 225).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Isoptericola.
OX   NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN   [1] {ECO:0000313|EMBL:AEG43743.1, ECO:0000313|Proteomes:UP000009236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Isoptericola variabilis 225.";
RL   Submitted (MAY-2011) 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         ECO:0000256|RuleBase:RU362051};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362051};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (bacterial route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004894, ECO:0000256|RuleBase:RU362051}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040,
CC       ECO:0000256|RuleBase:RU362051}.
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DR   EMBL; CP002810; AEG43743.1; -; Genomic_DNA.
DR   RefSeq; WP_013838135.1; NC_015588.1.
DR   AlphaFoldDB; F6FPV4; -.
DR   STRING; 743718.Isova_0959; -.
DR   KEGG; iva:Isova_0959; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_014312_6_1_11; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000009236; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   NCBIfam; TIGR01816; sdhA_forward; 1.
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; 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   ECO:0000256|RuleBase:RU362051};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR611281-4};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362051};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362051};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362051};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009236};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN          7..408
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          463..611
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        294
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT   MOD_RES         42
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ   SEQUENCE   611 AA;  67492 MW;  87CBA97F700B555A CRC64;
     MQTHQYDVVI VGAGGAGMRA ALEASKEART AVISKLYPTR SHTGAAQGGM CAALANVEED
     NWEWHTFDTI KGGDYLVDQD AAEIMAKEAI DAVLDLERMG LPFNRTPEGK IDQRRFGGHT
     RNHGEAAVRR ACYAADRTGH MILQTLYQNC VKQDVEFFNE FYVLDLLTDH DLTTEQIGDG
     EEVNATGVVA YDLATGEIHV FQAKAIIFAT GGAGKIFKTT SNAHTLTGDG MALAYRRGLP
     LEDMEFFQFH PTGLAGLGIL LSEAARGEGG ILRNADGERF MERYAPTIKD LAPRDIVARS
     MANEVREGRG AGPNKDYVLL DLTHLEPAHI DAKLPDITEF ARTYLGIEPY TEPVPVYPTA
     HYAMGGVPTN VDGEVLRDAR NVVKGLYAAG EVACVSVHGS NRLGTNSLLD INVFGKRAGR
     AAAAYARTVD RHRELPENPA GRVVEQLEEM RDRPDGERVA DVRRALQETM DANAQVFRTG
     ESLTQALSDI RELQKRYRNV SVQDKGKLFN TDLLEAIELG FLLDIAEVTV VAALNRKESR
     GGHYREDYPQ RDDANYMLHT MAYRRPTSAP DVADGTVKGY FDHVEEFGDY KVVLGSKPVT
     QTRYEPMERK Y
//
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