ID B2AXY9_PODAN Unreviewed; 648 AA. AC B2AXY9; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 86. 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=PODANS_1_9290 {ECO:0000313|EMBL:CAP69263.1}; OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) OS (Pleurage anserina). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora; OC Podospora anserina. OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP69263.1}; RN [1] {ECO:0000313|EMBL:CAP69263.1, ECO:0000313|Proteomes:UP000001197} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383 RC {ECO:0000313|Proteomes:UP000001197}, and S mat+ RC {ECO:0000313|EMBL:CAP69263.1}; RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77; RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M., RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V., RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M., RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D., RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B., RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H., RA Debuchy R., Wincker P., Weissenbach J., Silar P.; RT "The genome sequence of the model ascomycete fungus Podospora anserina."; RL Genome Biol. 9:R77.1-R77.22(2008). RN [2] {ECO:0000313|EMBL:CAP69263.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP69263.1}; RA Genoscope - CEA; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000001197} RP GENOME REANNOTATION. RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383 RC {ECO:0000313|Proteomes:UP000001197}; RX PubMed=24558260; DOI=10.1534/genetics.113.159988; RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A., RA Couloux A., Wincker P., Debuchy R., Silar P.; RT "Maintaining two mating types: Structure of the mating type locus and its RT role in heterokaryosis in Podospora anserina."; RL Genetics 197:421-432(2014). RN [4] {ECO:0000313|EMBL:CDP23282.1} RP NUCLEOTIDE SEQUENCE. RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E., RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.; RT "Maintaining two mating types: Structure of the mating type locus and its RT role in heterokaryosis in Podospora anserina."; RL Submitted (APR-2015) 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|PIRSR:PIRSR630664-51, 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 --------------------------------------------------------------------------- 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; CU633901; CAP69263.1; -; Genomic_DNA. DR EMBL; FO904936; CDP23282.1; -; Genomic_DNA. DR RefSeq; XP_001908590.1; XM_001908555.1. DR AlphaFoldDB; B2AXY9; -. DR STRING; 515849.B2AXY9; -. DR GeneID; 6193320; -. DR KEGG; pan:PODANSg5625; -. DR VEuPathDB; FungiDB:PODANS_1_9290; -. DR eggNOG; KOG2403; Eukaryota. DR HOGENOM; CLU_014312_6_1_1; -. DR OrthoDB; 551958at2759; -. DR UniPathway; UPA00223; UER01006. DR Proteomes; UP000001197; Chromosome 1. 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: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, ECO:0000256|PIRSR:PIRSR630664- KW 51}; 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:UP000001197}; 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 64..459 FT /note="FAD-dependent oxidoreductase 2 FAD binding" FT /evidence="ECO:0000259|Pfam:PF00890" FT DOMAIN 514..648 FT /note="Fumarate reductase/succinate dehydrogenase FT flavoprotein-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF02910" FT REGION 585..604 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 589..604 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 341 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1" FT BINDING 69..74 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51" FT BINDING 92..107 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51" FT BINDING 276 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51" FT BINDING 297 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51" FT BINDING 309 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51" FT BINDING 408 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51" FT BINDING 442 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51" FT BINDING 453 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51" FT BINDING 458..459 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51" FT MOD_RES 100 FT /note="Tele-8alpha-FAD histidine" FT /evidence="ECO:0000256|PIRSR:PIRSR611281-4" SQ SEQUENCE 648 AA; 70906 MW; FFA826023AE49EAB CRC64; MASSMAWRRL AAAPALPRAL RTPTQRAFST TRPAARVIAN GPLRAKEASP FVSSKYPVID HEYDAIVVGA GGAGLRAAFG LAEAGFNTAC ISKLFPTRSH TVAAQGGINA ALGNMHKDDW RWHMYDTVKG SDWLGDQDAI HYMTREAPAS IIELENYGCP FSRTEDGKIY QRAFGGQSKE YGKGGQAYRC CAAADRTGHA LLHTLYGQSL RHNTNYFIEY FAIDLIMQDG ECRGVLAYNQ EDGTLHRFLA NNTVLATGGY GRAYFSCTSA HTCTGDGMAM VARAGLPNQD LEFVQFHPTG IYGAGCLITE GARGEGGYLL NSEGERFMER YAPTAKDLAS RDVVSRSMTM EIRDGRGVGA EKDHIYLQLS HLPAEILAER LPGISETAGI FAGVDVRKQP IPVLPTVHYN MGGIPTRYTG EVLTVDESGN DKVVPGLFAC GEAACVSVHG ANRLGANSLL DLVVFGRAVA HTIRDNFTPG AKLKPVEADA GAAEIEMLDK IRTADGPKST AEIRLAMQKT MQRDVSVFRT QESLDEGVEK INQVDQTFSQ VGIKDRSMIW NSDLVETLEL RNLLTCAVQT ATAAANRKES RGAHAREDYP DRDDENWMKH TLTWQKPHGK VDLKYRRVIG TTLDENECKP VPPFKRVY //