GenomeNet

Database: UniProt
Entry: Q7QFL5_ANOGA
LinkDB: Q7QFL5_ANOGA
Original site: Q7QFL5_ANOGA 
ID   Q7QFL5_ANOGA            Unreviewed;       914 AA.
AC   Q7QFL5;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 5.
DT   27-MAR-2024, entry version 123.
DE   SubName: Full=AGAP000551-PA {ECO:0000313|EMBL:EAA06290.5};
GN   Name=1271673 {ECO:0000313|EnsemblMetazoa:AGAP000551-PA};
GN   ORFNames=AgaP_AGAP000551 {ECO:0000313|EMBL:EAA06290.5};
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA06290.5};
RN   [1] {ECO:0000313|EMBL:EAA06290.5, ECO:0000313|Proteomes:UP000007062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA06290.5,
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., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., 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., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   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:EAA06290.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA06290.5};
RG   The Anopheles Genome Sequencing Consortium;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAA06290.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA06290.5};
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:EAA06290.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA06290.5};
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:R5.1-R5.13(2007).
RN   [5] {ECO:0000313|EMBL:EAA06290.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA06290.5};
RG   VectorBase;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EnsemblMetazoa:AGAP000551-PA}
RP   IDENTIFICATION.
RC   STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP000551-PA};
RG   EnsemblMetazoa;
RL   Submitted (JAN-2021) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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; AAAB01008846; EAA06290.5; -; Genomic_DNA.
DR   RefSeq; XP_310532.5; XM_310532.5.
DR   AlphaFoldDB; Q7QFL5; -.
DR   STRING; 7165.Q7QFL5; -.
DR   PaxDb; 7165-AGAP000551-PA; -.
DR   EnsemblMetazoa; AGAP000551-RA; AGAP000551-PA; AGAP000551.
DR   GeneID; 1271673; -.
DR   KEGG; aga:AgaP_AGAP000551; -.
DR   VEuPathDB; VectorBase:AGAP000551; -.
DR   eggNOG; KOG0451; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; Q7QFL5; -.
DR   OMA; TPAQYYH; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000007062; Chromosome X.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007062};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          563..768
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   914 AA;  102565 MW;  6B5ABC437ABE5EC6 CRC64;
     MLGRLLLSRG YHSTKGVFGH RPRPTTRYEG LAAAVLDKRN ANANVYRWVE AYRNHGHRMA
     AIDPVKFHLA DEAASEPLPE LQYARYGLGA ADRIDPRGLL NVPAAQQPLS MAELDALLAR
     MYCGSCSIEL AFIESEQERE WVAGRYEQLF QHELTEGERR ELAELMLKSQ AFDQFLAVKF
     PTVKRYGGEG AESMMAFYWE LFRSAGEHEL RNVVIGMPHR GKLNVLTTMF GTRPAKIFKK
     FKGHPEFPAD AQAMCDIASH FHTSTDIIVG GKTFHLNMLH NPSHLEAVNP VSMGKARAKQ
     LALADGPYDT SGTDRRSKVL NVQVHGDAAF PGQGINQECL MMAAVPHYEV EGTVHLIVNN
     QVGFTTPAER GRSTRYVSDL AKAIMAPVVH VNGDDPEALA GVTQLAIEYR QKFGKDFFID
     LNCYRRWGHN ELDDPTVTNP LLYRVIHGRP SIPDRYAGRL IEAGVFDQQD VDAISNSHRN
     YLTAELAACE QYEPERSYFG GQWAGLQQPG DEVTVWNTGV DYRLLSHIGQ ESVRLPEGFN
     VHPHLQKTHI DARRKRIAEG QRIDWATAEA LAIGSLMYQG FNVRLSGEDV GRGTFAQRHA
     MLVDQQTNEI FIPLNAMAAA TPNAGRFELA NSILSEEAVL GFEYGMAIDS PNSLVLWEAQ
     FGDFFNGAQI IIDTFLVSGE TKWMVCNGLV MLLPHGYDGA ASEHSSCRVE RFLQMTDSRE
     TSPDGDAVNL QIINPSTPAQ YFHALRRQQI RNFRKPLLVV APKTLLRLSD CVSPHTDFAP
     GTHFQPVLPD PAPLDPKRVR RVVLCSGKHY YTLASERQAR QVTDVALVRV ESLCPFPVQA
     IRDELAKYAN AREFVWSQEE HRNMGAWTFV QPRFENMCER RIQYRGRPEA ATVAVGVSKW
     HVREAEDVIK TTLY
//
DBGET integrated database retrieval system