GenomeNet

Database: UniProt/TrEMBL
Entry: E0VZC3_PEDHC
LinkDB: E0VZC3_PEDHC
Original site: E0VZC3_PEDHC 
ID   E0VZC3_PEDHC            Unreviewed;       634 AA.
AC   E0VZC3;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   20-DEC-2017, entry version 48.
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=8235135 {ECO:0000313|VectorBase:PHUM530140-PA};
GN   ORFNames=Phum_PHUM530140 {ECO:0000313|EMBL:EEB18729.1};
OS   Pediculus humanus subsp. corporis (Body louse).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura;
OC   Pediculidae; Pediculus.
OX   NCBI_TaxID=121224 {ECO:0000313|Proteomes:UP000009046};
RN   [1] {ECO:0000313|EMBL:EEB18729.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB18729.1};
RA   Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA   Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA   Amedeo P., Strausberg R.;
RT   "Annotation of Pediculus humanus corporis strain USDA.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB18729.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB18729.1};
RG   The Human Body Louse Genome Consortium;
RA   Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT   "The genome of the human body louse.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000009046, ECO:0000313|VectorBase:PHUM530140-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA {ECO:0000313|Proteomes:UP000009046,
RC   ECO:0000313|VectorBase:PHUM530140-PA};
RX   PubMed=20566863; DOI=10.1073/pnas.1003379107;
RA   Kirkness E.F., Haas B.J., Sun W., Braig H.R., Perotti M.A.,
RA   Clark J.M., Lee S.H., Robertson H.M., Kennedy R.C., Elhaik E.,
RA   Gerlach D., Kriventseva E.V., Elsik C.G., Graur D., Hill C.A.,
RA   Veenstra J.A., Walenz B., Tubio J.M., Ribeiro J.M., Rozas J.,
RA   Johnston J.S., Reese J.T., Popadic A., Tojo M., Raoult D., Reed D.L.,
RA   Tomoyasu Y., Krause E., Mittapalli O., Margam V.M., Li H.M.,
RA   Meyer J.M., Johnson R.M., Romero-Severson J., Vanzee J.P.,
RA   Alvarez-Ponce D., Vieira F.G., Aguade M., Guirao-Rico S., Anzola J.M.,
RA   Yoon K.S., Strycharz J.P., Unger M.F., Christley S., Lobo N.F.,
RA   Seufferheld M.J., Wang N., Dasch G.A., Struchiner C.J., Madey G.,
RA   Hannick L.I., Bidwell S., Joardar V., Caler E., Shao R., Barker S.C.,
RA   Cameron S., Bruggner R.V., Regier A., Johnson J., Viswanathan L.,
RA   Utterback T.R., Sutton G.G., Lawson D., Waterhouse R.M., Venter J.C.,
RA   Strausberg R.L., Berenbaum M.R., Collins F.H., Zdobnov E.M.,
RA   Pittendrigh B.R.;
RT   "Genome sequences of the human body louse and its primary endosymbiont
RT   provide insights into the permanent parasitic lifestyle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:12168-12173(2010).
RN   [4] {ECO:0000313|VectorBase:PHUM530140-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|VectorBase:PHUM530140-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; DS235851; EEB18729.1; -; Genomic_DNA.
DR   RefSeq; XP_002431467.1; XM_002431422.1.
DR   STRING; 121225.PHUM530140-PA; -.
DR   EnsemblMetazoa; PHUM530140-RA; PHUM530140-PA; PHUM530140.
DR   GeneID; 8235135; -.
DR   KEGG; phu:Phum_PHUM530140; -.
DR   VectorBase; PHUM530140-RA; PHUM530140-PA; PHUM530140.
DR   CTD; 8235135; -.
DR   InParanoid; E0VZC3; -.
DR   KO; K00234; -.
DR   OMA; GDSPWEH; -.
DR   PhylomeDB; E0VZC3; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000009046; Partially assembled WGS sequence.
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: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; 1.20.58.100; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
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:UP000009046};
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   ECO:0000313|EMBL:EEB18729.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transit peptide {ECO:0000256|RuleBase:RU362051};
KW   Transport {ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    634       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5011412770.
FT   DOMAIN       30    427       FAD_binding_2. {ECO:0000259|Pfam:
FT                                PF00890}.
FT   DOMAIN      482    634       Succ_DH_flav_C. {ECO:0000259|Pfam:
FT                                PF02910}.
SQ   SEQUENCE   634 AA;  70119 MW;  B10C7B1D5F9D723C CRC64;
     MVQNVPDQIA LFFLFLCVQG QYQVIDHEFD AVVVGAGGAG LRAAFGLVAE GFNTAVITKL
     FPTRSHTVAA QGGINAALGN MEQDDWRWHM YDTVKGSDWL GDQDAIHYMT REAPKAVIEL
     ENYGMPFSRT DEGKIYQRAF GGQSLNFGKG GQAHRCCCVA DRTGHSLLHT LYGQSLRYDC
     NYFIEYFALD LIMDKNEKTC KGVIALCLED GSIHRFRAKN TVLATGGYGR AYFSCTSAHT
     CTGDGTAMIS RAGLHNEDLE FVQFHPTGIY GAGCLITEGC RGEGGYLINS EGERFMERYA
     PVAKDLASRD VVSRSMTIEI REGRGVGPEK DHVYLQLHHL PPEQLHTRLP GISETAMIFA
     GVDVTREPIP VLPTVHYNMG GIPTNYKGQV VTVDGVGNDV VVNGLYAAGE CACSSVHGAN
     RLGANSLLDL VVFGRACAKT IASENKPGEK TMELSDSDGE DSVTNLDNVR YANGSISVAD
     LRLKMQKTMQ NHAAVFRTQE TLAEGCEKMA KMYKELKNIK VYDRSLIWNS DLVEGLELQN
     LMINALQTII GAENRKESRG AHAREDFKDR IDEYNYSQPL ENQQPKSIEN HWRKHTLTCM
     NVDTGEVTIE YRPVIDKTLD ENECKTVPPA VRSY
//
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