ID Q06SM3_STECO Unreviewed; 494 AA. AC Q06SM3; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 09-DEC-2015, entry version 36. DE RecName: Full=Succinate dehydrogenase (quinone) {ECO:0000256|RuleBase:RU362051}; DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051}; DE Flags: Fragment; GN Name=SDHA {ECO:0000313|EMBL:ABF83576.1}; OS Stenella coeruleoalba (Striped dolphin) (Delphinus coeruleoalbus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Cetacea; OC Odontoceti; Delphinidae; Stenella. OX NCBI_TaxID=9737 {ECO:0000313|EMBL:ABF83576.1}; RN [1] {ECO:0000313|EMBL:ABF83576.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16984641; DOI=10.1186/1471-2199-7-32; RA Spinsanti G., Panti C., Lazzeri E., Marsili L., Casini S., Frati F., RA Fossi M.C.; RT "Selection of reference genes for quantitative RT-PCR studies in RT striped dolphin (Stenella coeruleoalba) skin biopsies."; RL BMC Mol. Biol. 7:32-32(2006). CC -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol. CC {ECO:0000256|RuleBase:RU362051}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU362051}; CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC FRD/SDH subfamily. {ECO:0000256|RuleBase:RU362051}. 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; DQ533607; ABF83576.1; -; mRNA. DR ProteinModelPortal; Q06SM3; -. DR HOVERGEN; HBG001461; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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-KW. DR Gene3D; 1.20.58.100; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR Gene3D; 3.90.700.10; -; 1. DR InterPro; IPR003953; FAD-binding_2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR003952; FRD_SDH_FAD_BS. DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C. DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat. 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; 2. 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 2: Evidence at transcript level; 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 Transport {ECO:0000256|RuleBase:RU362051}; KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}. FT DOMAIN 1 393 FAD_binding_2. {ECO:0000259|Pfam: FT PF00890}. FT DOMAIN 448 494 Succ_DH_flav_C. {ECO:0000259|Pfam: FT PF02910}. FT NON_TER 1 1 {ECO:0000313|EMBL:ABF83576.1}. FT NON_TER 494 494 {ECO:0000313|EMBL:ABF83576.1}. SQ SEQUENCE 494 AA; 53515 MW; 0DAA68A71A43F694 CRC64; VVVGAGGAGL RAAFGLSEAG FNTACVTKLF PTRSHTVAAQ GGINAALGNM EEDNWRWHFY DTVKGSDWLG DQDAIHYMTE QAPASVVELE NYGMPFSRTE DGKIYQRAFG GQSLKFGKGG QAHRCCCVAD RTGHSLLHTL YGRSLRYDTS YFVEYFALDL LMENGECRGV IALCIEDGSI HRIRAKNTVV ATGGYGRTYF SCTSAHTSTG DGTAMITRAG LPCQDLEFVQ FHPTGIYGAG CLITEGCRGE GGILINSQGE RFMERYAPVA KDLASRDVVS RSMTLEIREG RGCGPEKDHV YLQLHHLPPE QLAMRLPGIS ETAMIFAGVD VTKEPIPVLP TVHYNMGGIP TNYKGQVLKH VGGQDQVVPG LYACGEAACA SVHGANRLGA NSLLDLVVFG RACALSIAES CKPGDKVPLI KPNAGEESVM NLDKLRFANG SIRTSELRLN MQKSMQSHAA VFRVGSVLQE GCEKISKLYG DLKHLKTFDR GMVW //