ID A0A0L0USU3_9BASI Unreviewed; 652 AA. AC A0A0L0USU3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 27-MAR-2024, entry version 34. 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=PSTG_16555 {ECO:0000313|EMBL:KNE89971.1}; OS Puccinia striiformis f. sp. tritici PST-78. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia. OX NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNE89971.1, ECO:0000313|Proteomes:UP000054564}; RN [1] {ECO:0000313|Proteomes:UP000054564} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564}; RG The Broad Institute Genome Sequencing Platform; RA Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. 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}. 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:KNE89971.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJIL01000284; KNE89971.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0L0USU3; -. DR SMR; A0A0L0USU3; -. DR STRING; 1165861.A0A0L0USU3; -. DR OrthoDB; 551958at2759; -. DR UniPathway; UPA00223; UER01006. DR Proteomes; UP000054564; 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 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:UP000054564}; 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}; KW Ubiquinone {ECO:0000313|EMBL:KNE89971.1}. FT DOMAIN 64..461 FT /note="FAD-dependent oxidoreductase 2 FAD binding" FT /evidence="ECO:0000259|Pfam:PF00890" FT DOMAIN 516..652 FT /note="Fumarate reductase/succinate dehydrogenase FT flavoprotein-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF02910" FT REGION 586..606 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 589..606 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 342 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1" FT MOD_RES 100 FT /note="Tele-8alpha-FAD histidine" FT /evidence="ECO:0000256|PIRSR:PIRSR611281-4" SQ SEQUENCE 652 AA; 70954 MW; 8AB6E9FB371F9F0A CRC64; MLRSKILNRI KPATSSLSLA KRSFTSSPSC ARIISSQPVK ASESSSIASK FSSGNYPIID HEYDAIVVGA GGAGLRAAFG LAEAGLNTAC ITKLFPTRSH TVAAQGGVNA ALGNMTEDDW RWHMYDTVKG SDWLGDQDAI HYMCKEAPQA VIELEHFGVP FSRTKEGKIY QRAFGGQSLK YGKGGQAYRC AAAADRTGHA ILHTLYGQSL RHNTNFFVEF FALDLIMDDS GNCVGVTAYN QEDGTLHRFR AHQTVLATGG YGRAYFSCTS AHTCSGDGNA MVTRAGLPLQ DLEFVQFHPT GIYGAGCLIT EGSRGEGGYL LNSQGERFME RYAPTAKDLA SRDVVSRSMT IEIREGRGVG PDKDHCYLQL SHLPPEVLHE RLPGISETAA IFAGVDVTKE PIPVLPTVHY NMGGIPTNYH GQVITQDSKT GADKIVGGLY AAGEAACVSV HGANRLGANS LLDIVVFGRA CAKHISANME PGKPHKPMPE DAGMKSIEDL DKLRNAKGPK PTAQIRNDMQ RVMQNDAAVF RTQSSLAEGV TKIHKVVDSF KDVGVTDRSM IWNTDLVETL ELRNLLTCAA QTMSSAEARK ESRGAHARED FPEREDDTWM KHTLSWHNPE SGDPVKLTYR DVISSTLDEN ECKSVPPFKR TY //