ID A0A0L0USU3_9BASI Unreviewed; 652 AA. AC A0A0L0USU3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 05-JUN-2019, entry version 19. 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., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA 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 CC (SDH) that is involved in complex II of the mitochondrial electron CC transport chain and is responsible for transferring electrons from CC succinate to ubiquinone (coenzyme Q). CC {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|RuleBase:RU362051}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC fumarate 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|RuleBase:RU362051}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblFungi; KNE89971; KNE89971; PSTG_16555. DR OrthoDB; 606981at2759; -. 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: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; -; 1. DR Gene3D; 3.90.700.10; -; 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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf. DR InterPro; IPR011281; Succ_DH_flav_su_fwd. DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg. DR Pfam; PF00890; FAD_binding_2; 1. DR Pfam; PF02910; Succ_DH_flav_C; 1. DR SUPFAM; SSF46977; SSF46977; 1. DR SUPFAM; SSF51905; SSF51905; 1. DR SUPFAM; SSF56425; SSF56425; 1. DR TIGRFAMs; TIGR01816; sdhA_forward; 1. DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1. DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054564}; KW Electron transport {ECO:0000256|RuleBase:RU362051}; KW FAD {ECO:0000256|RuleBase:RU362051}; KW Flavoprotein {ECO:0000256|RuleBase:RU362051}; KW Membrane {ECO:0000256|RuleBase:RU362051}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362051}; KW Reference proteome {ECO:0000313|Proteomes:UP000054564}; KW Transit peptide {ECO:0000256|RuleBase:RU362051}; KW Transport {ECO:0000256|RuleBase:RU362051}; KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}; KW Ubiquinone {ECO:0000313|EMBL:KNE89971.1}. FT DOMAIN 64 461 FAD_binding_2. {ECO:0000259|Pfam: FT PF00890}. FT DOMAIN 516 652 Succ_DH_flav_C. {ECO:0000259|Pfam: FT PF02910}. FT REGION 586 606 Disordered. {ECO:0000256|MobiDB-lite: FT A0A0L0USU3}. FT COMPBIAS 589 606 Polyampholyte. {ECO:0000256|MobiDB-lite: FT A0A0L0USU3}. 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 //