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Database: UniProt
Entry: A0A1R1SNS9_9ACTN
LinkDB: A0A1R1SNS9_9ACTN
Original site: A0A1R1SNS9_9ACTN 
ID   A0A1R1SNS9_9ACTN        Unreviewed;       650 AA.
AC   A0A1R1SNS9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:OMI39954.1};
DE            EC=1.3.5.1 {ECO:0000313|EMBL:OMI39954.1};
GN   Name=sdhA {ECO:0000313|EMBL:OMI39954.1};
GN   ORFNames=SPAR_08361 {ECO:0000313|EMBL:OMI39954.1};
OS   Streptomyces sparsogenes DSM 40356.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI39954.1, ECO:0000313|Proteomes:UP000186168};
RN   [1] {ECO:0000313|EMBL:OMI39954.1, ECO:0000313|Proteomes:UP000186168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI39954.1,
RC   ECO:0000313|Proteomes:UP000186168};
RA   Coyne S., Seebeck F.P.;
RT   "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:OMI39954.1}.
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DR   EMBL; ASQP01000121; OMI39954.1; -; Genomic_DNA.
DR   RefSeq; WP_065964022.1; NZ_ASQP01000121.1.
DR   AlphaFoldDB; A0A1R1SNS9; -.
DR   STRING; 67365.GCA_001704635_07397; -.
DR   Proteomes; UP000186168; Unassembled WGS sequence.
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   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; 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; 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   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF89; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 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.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:OMI39954.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186168}.
FT   DOMAIN          10..432
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          499..596
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   REGION          304..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        324
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   650 AA;  71553 MW;  0F1A9CC346B6FA2A CRC64;
     MTQVERQAWD VVVVGAGGAG LRAAIEAREQ GKRCAVICKS LFGKAHTVMA EGGIAASMGN
     VNEGDNWQVH FRDTMRGGKF LNHWRMAELH AQEAPDRVWE LETWGALFDR TPDGRISQRN
     FGGHEYPRLA HVGDRTGLEL IRTLQQKIVA LQQEDKAEFG DYEARLKVFQ EYTVTRVIKD
     EDGERVAGVF GYERESGRFF VIEAPAVVLA TGGIGKSFKV TSNSWEYTGD GHALALLAGA
     PLVNMEFVQF HPTGMVWPPS VKGILVTESV RGDGGVLRNS DGKRFMFDYI PDVFKEKYAQ
     TEDEADRWYE DPDNNRRPPE LLPRDEVARA INAEVKAGRG SPHGGVFLDV STRMPAEVIK
     RRLPSMHHQF KELADVDITA EPMEVGPTCH YVMGGVDVDP DTTAAAGVPG LFAAGEVAGG
     MHGSNRLGGN SLSDLLVFGR RAGLYAARYA EEAAGAGRRP APDDAQVDLA AAEALRPFSA
     EGGDPGLAAG PAENPYTLHQ ELQQTMNDLV GIIRRAGEME EALQRLANLR ARARRAGVEG
     HRQFNPGWHL AIDLRNMLLV SECVARAALE RTESRGGHTR DDYPEMDREW RPVNLVCRLA
     DPSGGLAAPD ARQGQIRLER HRTPPIRPDL LGLFEKDELA KYLTDEELTQ
//
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