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Database: UniProt/TrEMBL
Entry: Q7QDV0_ANOGA
LinkDB: Q7QDV0_ANOGA
Original site: Q7QDV0_ANOGA 
ID   Q7QDV0_ANOGA            Unreviewed;       659 AA.
AC   Q7QDV0;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 4.
DT   23-MAY-2018, entry version 117.
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=1272618 {ECO:0000313|VectorBase:AGAP010429-PA};
GN   ORFNames=AgaP_AGAP010429 {ECO:0000313|EMBL:EAA07202.4};
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA07202.4, ECO:0000313|Proteomes:UP000007062};
RN   [1] {ECO:0000313|EMBL:EAA07202.4, ECO:0000313|Proteomes:UP000007062, ECO:0000313|VectorBase:AGAP010429-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA07202.4,
RC   ECO:0000313|Proteomes:UP000007062};
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B.,
RA   Lai Z., Kraft C.L., Abril J.F., Anthouard V., Arensburger P.,
RA   Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V.,
RA   Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S.,
RA   Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M.,
RA   Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I.,
RA   Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z.,
RA   Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R.,
RA   Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E.,
RA   Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F.,
RA   Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R.,
RA   Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C.,
RA   Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V.,
RA   Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D.,
RA   Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H.,
RA   Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A.,
RA   Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F.,
RA   Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S.,
RA   Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C.,
RA   Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
RN   [2] {ECO:0000313|EMBL:EAA07202.4}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA07202.4};
RG   The Anopheles Genome Sequencing Consortium;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAA07202.4}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA07202.4};
RX   PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA   Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT   "The Anopheles gambiae genome: an update.";
RL   Trends Parasitol. 20:49-52(2004).
RN   [4] {ECO:0000313|EMBL:EAA07202.4}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA07202.4};
RX   PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA   Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA   Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT   "Update of the Anopheles gambiae PEST genome assembly.";
RL   Genome Biol. 8:R5-R5(2007).
RN   [5] {ECO:0000313|EMBL:EAA07202.4}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA07202.4};
RG   VectorBase;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|VectorBase:AGAP010429-PA}
RP   IDENTIFICATION.
RC   STRAIN=PEST {ECO:0000313|VectorBase:AGAP010429-PA};
RG   VectorBase;
RL   Submitted (FEB-2017) to UniProtKB.
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: 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   -!- 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}.
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DR   EMBL; AAAB01008849; EAA07202.4; -; Genomic_DNA.
DR   RefSeq; XP_311518.4; XM_311518.4.
DR   ProteinModelPortal; Q7QDV0; -.
DR   STRING; 7165.AGAP010429-PA; -.
DR   EnsemblMetazoa; AGAP010429-RA; AGAP010429-PA; AGAP010429.
DR   GeneID; 1272618; -.
DR   KEGG; aga:AgaP_AGAP010429; -.
DR   VectorBase; AGAP010429-RA; AGAP010429-PA; AGAP010429.
DR   eggNOG; KOG2403; Eukaryota.
DR   eggNOG; COG1053; LUCA.
DR   HOGENOM; HOG000160475; -.
DR   InParanoid; Q7QDV0; -.
DR   KO; K00234; -.
DR   OMA; GDSPWEH; -.
DR   OrthoDB; EOG091G041Z; -.
DR   PhylomeDB; Q7QDV0; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000007062; Chromosome 3L.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR   GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 2.
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; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007062};
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:UP000007062};
KW   Transit peptide {ECO:0000256|RuleBase:RU362051};
KW   Transport {ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN       59    453       FAD_binding_2. {ECO:0000259|Pfam:
FT                                PF00890}.
FT   DOMAIN      508    659       Succ_DH_flav_C. {ECO:0000259|Pfam:
FT                                PF02910}.
SQ   SEQUENCE   659 AA;  72205 MW;  F4A1F2D12C131A1B CRC64;
     MSGMIRLPTV LAKNALSAVR GLTAGTSQRN LHFTVGQNNA KSNPDAISRE YPVVDHTYDA
     VVVGAGGAGL RAAFGLVAEG FKTAVITKLF PTRSHTVAAQ GGINAALGNM EEDDWKWHMY
     DTVKGSDWLG DQDAIHYMTR EAPKAVIELE NYGMPFSRTP DGKIYQRAFG GQSLKYGKGG
     QAHRCCCVAD RTGHSLLHTL YGQSLSYDCN YFIEYFAMDL LMQNGECVGV IAMNLEDGSI
     HRFRAKNTVL ATGGYGRAYF SCTSAHTCTG DGTAMVARAG LPSEDLEFVQ FHPTGIYGAG
     CLITEGCRGE GGYLINSQGE RFMERYAPVA KDLASRDVVS RSMTIEIREG RGCGPEKDHV
     YLQLHHLPPE QLAQRLPGIS ETAMIFAGVD VTREPIPVLP TVHYNMGGVP TNYKGQVLTT
     QNGADRVVPG LYACGEAACS SVHGANRLGA NSLLDLVVFG RACAKTIAEE NRPGEKVQDL
     KPNAGEASVA NLDWVRNADG QVPTSTLRLN MQKTMQTHAA VFREEKTLQE GVRKMGDIYK
     TIKDVKVSDR SLVWNSDLVE TLELQNLLLN ANMTIVAAEN RKESRGAHAR EDYKQRVDEY
     DFSKPLEGQQ KKPVEEHWRK HTLTWIDPAT GNVTIDYRPV IDETLSEECA TVPPAIRSY
//
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