ID J4IBP9_9APHY Unreviewed; 639 AA.
AC J4IBP9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial {ECO:0000256|RuleBase:RU362051};
DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051};
GN ORFNames=FIBRA_07243 {ECO:0000313|EMBL:CCM05041.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM05041.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM05041.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM05041.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
CC -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH)
CC that is involved in complex II of the mitochondrial electron transport
CC chain and is responsible for transferring electrons from succinate to
CC ubiquinone (coenzyme Q). {ECO:0000256|RuleBase:RU362051}.
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|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 (eukaryal route): step 1/1.
CC {ECO:0000256|RuleBase:RU362051}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU362051}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU362051}; Matrix side
CC {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; HE797177; CCM05041.1; -; Genomic_DNA.
DR RefSeq; XP_012184324.1; XM_012328934.1.
DR AlphaFoldDB; J4IBP9; -.
DR STRING; 599839.J4IBP9; -.
DR GeneID; 24099952; -.
DR HOGENOM; CLU_014312_6_1_1; -.
DR InParanoid; J4IBP9; -.
DR OrthoDB; 551958at2759; -.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; 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:UP000006352};
KW Transit peptide {ECO:0000256|RuleBase:RU362051};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT DOMAIN 53..448
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 503..639
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 330
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT MOD_RES 89
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ SEQUENCE 639 AA; 70214 MW; 5328D40CDFC3AB4E CRC64;
MLRTSLPKAL RASQRSFHSS APARRVVATN PVKAQEVPSW ASGNYPLIEH EYDAIVVGAG
GAGLRAAFGL AEAGFNTACI TKLFPTRSHT VAAQGGINAA LGNMTEDDWR WHMYDTVKGS
DWLGDQDAIH YMCREAPRTV IELEHFGVPF SRTKEGKIYQ RAFGGQSLKY GKGGQAYRCA
AAADRTGHAL LHTLYGQSLR HNTNFFIEYF ALDLIMQDGE CVGVIALNME DGTLHRFRAH
KTVLATGGYG RAYFSCTSAH TCSGDGNAMV ARAGLPLQDS EFVQFHPTGI YGAGCLITEG
SRGEGGYLLN SEGERFMERY APTAKDLASR DVVSRSMTIE IREGRGVGPE KDHIYLQLSH
LPPEVLHERL PGISETAAIF TGVDVTKEPI PVLPTVHYNM GGIPTKYTGE VITVDESGKD
KVVPGLYAAG EAACVSVHGA NRLGANSLLD IVVFGRACAH HIKETLTPGK PHKEIPQEAG
LESIEFLDKI RKSDGPLPTA KIRLDMQKAM QADAAVFRTQ ESLDEGVQKL RAIYKSFDNV
GIKDRSMIWN SDLVETLELR NLLQCAVQTI TAAAARKESR GAHAREDFPE RDDEKWMKHT
LTWQHDVTSP EVDIKYRGVI DQTLDENECK PVPPFKRVY
//
