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Database: UniProt
Entry: A0A1K2FT62_9ACTN
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ID   A0A1K2FT62_9ACTN        Unreviewed;       584 AA.
AC   A0A1K2FT62;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   Name=sdhA_1 {ECO:0000313|EMBL:SFY50899.1};
GN   ORFNames=STEPF1_04155 {ECO:0000313|EMBL:SFY50899.1};
OS   Streptomyces sp. F-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=463642 {ECO:0000313|EMBL:SFY50899.1, ECO:0000313|Proteomes:UP000095403};
RN   [1] {ECO:0000313|EMBL:SFY50899.1, ECO:0000313|Proteomes:UP000095403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Streptomyces sp. F1 {ECO:0000313|EMBL:SFY50899.1};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FKJI03000010; SFY50899.1; -; Genomic_DNA.
DR   RefSeq; WP_070026210.1; NZ_FKJI03000010.1.
DR   AlphaFoldDB; A0A1K2FT62; -.
DR   OrthoDB; 9805351at2; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000095403; 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: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; PR00368; FADPNR.
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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000095403};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN          7..400
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          454..584
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   COILED          467..494
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        286
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   584 AA;  64902 MW;  CBB0C1D6D4355709 CRC64;
     MKIHKYDTVI VGAGGAGMRA AIEATKRSRT AVLTKLYPTR SHTGAAQGGM AAALANVEED
     NWEWHTFDTI KGGDYLVDQD AAEILAKEAI DAVLDLEKMG LPFNRTPNGT IDQRRFGGHS
     RNHGEAPVRR ACYAADRTGH MILQTLYQNC VKEGVEFFNE FYVLDQLISE VDGVKKSAGV
     VAYELATGEI HIFQAKSVIY ASGGTGKFFK VTSNAHTLTG DGQAACYRRG LPLEDMEFFQ
     FHPTGIWRMG ILLTEGARGE GGILRNKDGE RFMEKYAPVM KDLASRDVVS RSIYTEIREG
     RGCGPEGDHV YLDLTHLPPE QLDAKLPDIT EFARTYLGIE PYTDPIPIQP TAHYAMGGIP
     TNVEGEVLAD NTTVVPGLYA AGEVACVSVH GANRLGTNSL LDINVFGRRA GIAAAEYAHK
     ADFVELPENP ESFVVETIER LRNSTGNERV ATLRRELQET MDANVMVFRT EQTIKTAVEK
     IAELRERYKN VSIQDKGKRF NTDLLEAIEL GNLLDLAEVM ATSALARKES RGGHYREDYP
     NRDDVNFMRH TMAYREVGDD GTESIRLDYK PVVQTRYQPM ERKY
//
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