ID A0A5A4S6I0_9ENTR Unreviewed; 569 AA. AC A0A5A4S6I0; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 07-OCT-2020, entry version 6. DE RecName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000256|ARBA:ARBA00019965, ECO:0000256|RuleBase:RU362051}; DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU362051}; GN Name=sdhA {ECO:0000313|EMBL:BBK13306.1}; GN ORFNames=TMSI_36980 {ECO:0000313|EMBL:BBK13306.1}; OS Klebsiella quasipneumoniae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=1463165 {ECO:0000313|EMBL:BBK13306.1, ECO:0000313|Proteomes:UP000325882}; RN [1] {ECO:0000313|EMBL:BBK13306.1, ECO:0000313|Proteomes:UP000325882} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SNI47 {ECO:0000313|EMBL:BBK13306.1, RC ECO:0000313|Proteomes:UP000325882}; RA Suzuki Y., Kubota H., Ida M., Kato R., Suzuki J., Sadamasu K.; RT "Multiple beta-lactam-resistance gene-carrying plasmid harboured by RT Klebsiella quasipneumoniae isolated from urban sewage in Japan."; RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are CC responsible for the catalysis of fumarate and succinate CC interconversion; the fumarate reductase is used in anaerobic growth, CC and the succinate dehydrogenase is used in aerobic growth. CC {ECO:0000256|ARBA:ARBA00002054}. 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|ARBA:ARBA00000030, CC 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 (bacterial route): step 1/1. CC {ECO:0000256|ARBA:ARBA00004894, ECO:0000256|RuleBase:RU362051}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|ARBA:ARBA00004515, ECO:0000256|RuleBase:RU362051}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004515, CC ECO:0000256|RuleBase:RU362051}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004515, ECO:0000256|RuleBase:RU362051}. CC Membrane {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004287}. CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040, CC 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; AP019687; BBK13306.1; -; Genomic_DNA. DR UniPathway; UPA00223; UER01005. DR Proteomes; UP000325882; Chromosome. DR GO; GO:0005886; C:plasma 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 Cell inner membrane {ECO:0000256|RuleBase:RU362051}; KW Cell membrane {ECO:0000256|RuleBase:RU362051}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU362051}; FAD {ECO:0000256|RuleBase:RU362051}; 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 Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, KW ECO:0000256|RuleBase:RU362051}. FT DOMAIN 1..386 FT /note="FAD_binding_2" FT /evidence="ECO:0000259|Pfam:PF00890" FT DOMAIN 441..569 FT /note="Succ_DH_flav_C" FT /evidence="ECO:0000259|Pfam:PF02910" SQ SEQUENCE 569 AA; 62609 MW; 91681C96B354E4CB CRC64; MRAALQISQS GQTCALLSKV FPTRSHTVSA QGGITVALGN SHEDNWEWHM YDTVKGSDYI GDQDAIEYMC KTGPEAILEL EHMGLPFSRL DDGRIYQRPF GGQSKNFGGE QAARTAAAAD RTGHALLHTL YQQNLKNHTT IFSEWYALDL VKNQDGAVVG CTALCIETGE VVYFKARATV LATGGAGRIY QSTTNAHINT GDGVGMAIRA GVPVQDMEMW QFHPTGIAGA GVLVTEGCRG EGGYLLNKHG ERFMERYAPN AKDLAGRDVV ARSIMIEIRE GRGCDGPWGP HAKLKLDHLG KEVLESRLPG ILELSRTFAH VDPVKEPIPV IPTCHYMMGG IPTKVTGQAL TVNEKGEDVV IPGLFAVGEI ACVSVHGANR LGGNSLLDLV VFGRAAGLHL QESIAEQGTL RDASESDIEG SLDRLNRWNN TRSGEDPVAI RKALQECMQH NFSVFREGDA MHKGLEQLKV IRERLKNARL DDTSSEFNTQ RVECLELDNL METAYATAVS ANFRTESRGA HSRFDFPDRD DENWLCHSLY LPESESMTRR SVNMEPKLRP AFPPKIRTY //