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Database: UniProt
Entry: A0A1N7SS39_9BURK
LinkDB: A0A1N7SS39_9BURK
Original site: A0A1N7SS39_9BURK 
ID   A0A1N7SS39_9BURK        Unreviewed;       602 AA.
AC   A0A1N7SS39;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Fumarate reductase flavoprotein subunit {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN2476_770003 {ECO:0000313|EMBL:SIT50275.1};
OS   Paraburkholderia piptadeniae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT50275.1, ECO:0000313|Proteomes:UP000195569};
RN   [1] {ECO:0000313|EMBL:SIT50275.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM 7183 {ECO:0000313|EMBL:SIT50275.1};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CYGY02000077; SIT50275.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N7SS39; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000195569; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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: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.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          9..391
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          445..567
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   REGION          580..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   602 AA;  65454 MW;  A4F3F8C786655C92 CRC64;
     MNIAHIRTDI LILGSGGAGL FAALHAHQTA PQLSITVAVK GLLGKCGCTR MVQGGYNVAL
     APGDSVERHF MDTIEGSKWL SNQDLAWTLV STAVERVREL ENELGCFFDR NPDGSIHQKA
     FAGQTFDRTV HKGDLTGIEI INRLAEQVWS RGINRLEEHR AIELIRSRDG KSLAGVLMID
     MRSGQFVFVQ ARAVLLATGG GPTMYKFHTP SGDKSCDGLA MALRAGLPLR DMEMVQFHPT
     GLLAGSHTRM TGTVLEEGLR GAGGHLLNGD KERFMHRYDA RGERATRDIV SRGIYSEMRE
     GRTSPNGGVY IQMGHLGPDK VRKQFKGMVE RCADCGFDLA GGLVEVVPTA HYMMGGVVFQ
     TDCRTELTGL FAAGEDTGGV HGANRLGGNG VANSTVFGGI AGDSMATWVS EQGQHHAPDD
     DAIQAAISEA EAPFKQNGKD LENIRESLYE CMWKDVGISR HGDGLLRARA ALRDLYGQLM
     RTGVADGDRA LNLQWHDWLN LKNLISVSQV ITEAAIAREN SRGAHFREDF PDAGDLTRSA
     FTTVRRQQGE ICISQEPVTF TRVKPGETIL DEREKSLETG AVRGLKSTKA TKYGAPEGVA
     KR
//
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