ID   B4MYF9_DROWI            Unreviewed;       661 AA.
AC   B4MYF9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 105.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial {ECO:0000256|RuleBase:RU362051};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051};
GN   Name=Dwil\GK22213 {ECO:0000313|EMBL:EDW77148.1};
GN   Synonyms=dwil_GLEANR_5314 {ECO:0000313|EMBL:EDW77148.1}, GK22213
GN   {ECO:0000313|EMBL:EDW77148.1};
GN   ORFNames=Dwil_GK22213 {ECO:0000313|EMBL:EDW77148.1};
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW77148.1, ECO:0000313|Proteomes:UP000007798};
RN   [1] {ECO:0000313|EMBL:EDW77148.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14030-0811.24 {ECO:0000313|EMBL:EDW77148.1};
RA   Remington K., Strausberg R., Sutton G., Walenz B., Johnson J.,
RA   Utterback T., Venter J.C.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDW77148.1, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#14030-0811.24 {ECO:0000313|EMBL:EDW77148.1}, and Tucson
RC   14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 Genomes Consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [3] {ECO:0000313|EMBL:EDW77148.1, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#14030-0811.24 {ECO:0000313|EMBL:EDW77148.1}, and Tucson
RC   14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
RX   PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA   Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT   "Assembly reconciliation.";
RL   Bioinformatics 24:42-45(2008).
RN   [4] {ECO:0000313|EMBL:EDW77148.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14030-0811.24 {ECO:0000313|EMBL:EDW77148.1};
RG   FlyBase;
RL   Submitted (NOV-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 = fumarate + a quinol;
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|PIRSR:PIRSR611281-3};
CC       Note=Flavinylated by SdhE, about 5% flavinylation occurs in the absence
CC       of SdhE. {ECO:0000256|PIRSR:PIRSR611281-3};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (eukaryal route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004788, ECO:0000256|RuleBase:RU362051}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU362051};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443,
CC       ECO:0000256|RuleBase:RU362051}; Matrix side
CC       {ECO:0000256|ARBA:ARBA00004443, 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}.
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DR   EMBL; CH963894; EDW77148.1; -; Genomic_DNA.
DR   EMBL; CH963894; KRF98587.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4MYF9; -.
DR   SMR; B4MYF9; -.
DR   STRING; 7260.B4MYF9; -.
DR   GeneID; 6643359; -.
DR   KEGG; dwi:6643359; -.
DR   eggNOG; KOG2403; Eukaryota.
DR   HOGENOM; CLU_014312_6_1_1; -.
DR   OMA; PTGIWRM; -.
DR   OrthoDB; 71672at2759; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045273; C:respiratory chain complex II (succinate dehydrogenase); IEA:EnsemblMetazoa.
DR   GO; GO:0009055; F:electron transfer activity; IEA:TreeGrafter.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0160308; F:succinate dehydrogenase (FAD) activity; IEA:InterPro.
DR   GO; GO:0008177; F:succinate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IEA:TreeGrafter.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   FunFam; 3.90.700.10:FF:000001; Mitochondrial succinate dehydrogenase flavoprotein subunit; 1.
DR   FunFam; 4.10.80.40:FF:000004; Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial; 1.
DR   FunFam; 3.50.50.60:FF:000482; Succinate dehydrogenase complex, subunit A, flavoprotein (Fp); 1.
DR   FunFam; 3.50.50.60:FF:001062; Succinate dehydrogenase complex, subunit A, flavoprotein (Fp); 1.
DR   FunFam; 1.20.58.100:FF:000001; Succinate dehydrogenase flavoprotein subunit (SdhA); 1.
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-dep_OxRdtase_2_FAD-bd.
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:PIRSR611281-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR611281-
KW   3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362051};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362051};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007798};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
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          60..455
FT                   /note="FAD-dependent oxidoreductase 2 FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          510..661
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        337
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT   BINDING         65..70
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-3"
FT   BINDING         88..103
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-3"
FT   BINDING         272
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-3"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-2"
FT   BINDING         305
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-2"
FT   BINDING         404
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-2"
FT   BINDING         438
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-3"
FT   BINDING         449
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-2"
FT   BINDING         454..455
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-3"
FT   MOD_RES         96
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ   SEQUENCE   661 AA;  72312 MW;  9EAD3DE56EE1571C CRC64;
     MSGIMRVPSI LAKNAVASMH RVAAVASQRS YHITHGRHQA TAANPDKISK QYPIVDHSFD
     AIVVGAGGAG LRAAFGLVAE GFKTAVITKL FPTRSHTIAA QGGINAALGN MEEDDWKWHM
     YDTVKGSDWL GDQDAIHYMT REAPKAVIEL ENYGMPFSRT QDGKIYQRAF GGQSLKFGKG
     GQAHRCCAVA DRTGHSLLHT LYGQSLSYDC NYFVEYFALD LIFEDGECRG VLALNLEDGT
     LHRFRAQNTV MATGGYGRAF FSCTSAHTCT GDGTAMVARQ GLPSQDLEFV QFHPTGIYGA
     GCLITEGCRG EGGYLINSKG ERFMERYAPV AKDLASRDVV SRSMTIEIME GRGVGPEKDH
     VYLQLHHLPP KQLAERLPGI SETAMIFAGV DVTREPIPVL PTVHYNMGGI PTNYRGQVIT
     IDKDGKDVIV PGLYAAGEAA SSSVHGANRL GANSLLDLVV FGRACAKTIA EENKPGAPAP
     KLKDNAGEAS VANLDKLRHA NGQITTADLR LKMQKTMQGH AAVFRDGPIL QKGVAKMQEV
     YKEFKDVKVV DKSLIWNSDL VETLELQNLL ANAQMTIVGA EARKESRGAH AREDFKTRID
     EYDYSKPLEG QEKVPVEKHW RKHTLSWVCN DNGDVQLDYR NVIDTTLDNE VSTVPPAIRS
     Y
//