ID CISY2_AEDAE Reviewed; 467 AA. AC Q16P20; A6KW11; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 103. DE RecName: Full=Probable citrate synthase 2, mitochondrial; DE EC=2.3.3.16; DE Flags: Precursor; GN ORFNames=AAEL011789; OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; OC Culicinae; Aedini; Aedes; Stegomyia. OX NCBI_TaxID=7159; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LVPib12; RX PubMed=17510324; DOI=10.1126/science.1138878; RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J., RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F., RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P., RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L., RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J., RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E., RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I., RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H., RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S., RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P., RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J., RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W., RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O., RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R., RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B., RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T., RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.; RT "Genome sequence of Aedes aegypti, a major arbovirus vector."; RL Science 316:1718-1723(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); CC Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10117}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate CC from oxaloacetate: step 1/2. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of CC oxidative metabolism. CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}. 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; CH477799; EAT36098.1; -; Genomic_DNA. DR EMBL; CH477799; EAT36099.1; -; Genomic_DNA. DR RefSeq; XP_001655738.1; XM_001655688.1. DR RefSeq; XP_001655739.1; XM_001655689.1. DR AlphaFoldDB; Q16P20; -. DR SMR; Q16P20; -. DR STRING; 7159.Q16P20; -. DR PaxDb; 7159-AAEL011789-PB; -. DR EnsemblMetazoa; AAEL011789-RC; AAEL011789-PC; AAEL011789. DR EnsemblMetazoa; AAEL011789-RD; AAEL011789-PD; AAEL011789. DR GeneID; 5575386; -. DR KEGG; aag:5575386; -. DR VEuPathDB; VectorBase:AAEL011789; -. DR eggNOG; KOG2617; Eukaryota. DR HOGENOM; CLU_022049_2_1_1; -. DR InParanoid; Q16P20; -. DR OMA; VLEWLFK; -. DR OrthoDB; 3513214at2759; -. DR PhylomeDB; Q16P20; -. DR UniPathway; UPA00223; UER00717. DR Proteomes; UP000008820; Chromosome 3. DR Proteomes; UP000682892; Unassembled WGS sequence. DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB. DR GO; GO:0004108; F:citrate (Si)-synthase activity; ISS:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB. DR GO; GO:0006101; P:citrate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR CDD; cd06105; ScCit1-2_like; 1. DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1. DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1. DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub. DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub. DR InterPro; IPR002020; Citrate_synthase. DR InterPro; IPR019810; Citrate_synthase_AS. DR InterPro; IPR010109; Citrate_synthase_euk. DR InterPro; IPR036969; Citrate_synthase_sf. DR NCBIfam; TIGR01793; cit_synth_euk; 1. DR PANTHER; PTHR11739; CITRATE SYNTHASE; 1. DR PANTHER; PTHR11739:SF8; CITRATE SYNTHASE, MITOCHONDRIAL; 1. DR Pfam; PF00285; Citrate_synt; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR SUPFAM; SSF48256; Citrate synthase; 1. DR PROSITE; PS00480; CITRATE_SYNTHASE; 1. PE 3: Inferred from homology; KW Mitochondrion; Reference proteome; Transferase; Transit peptide; KW Tricarboxylic acid cycle. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..467 FT /note="Probable citrate synthase 2, mitochondrial" FT /id="PRO_0000291602" FT ACT_SITE 303 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT ACT_SITE 349 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT ACT_SITE 404 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" SQ SEQUENCE 467 AA; 51641 MW; 402BB11312107CB9 CRC64; MALSRIYSSK LASANKNLLP VITTYVRNAS DSTDLKAVLS EKIPKEQERV KNFRKQFGAT KVGEVTVDMM YGGMRGIKGL VCETSVLDPD EGIRFRGLSI PECQKVLPKA PGGAEPLPEG LFWLLITGDV PTKAQVDALS REWANRAALP SHVVTMLNNM PTTLHPMSQL SCAVTALNHE SKYAKAYSEG VHKSKYWEYV YEDSMDLIAK LPVVAATIYR NTYRDGKGIG AIDPKKDWSA NFTKMLGYED EQFTELMRLY LTIHSDHEGG NVSAHTVHLV GSALSDPYLS FAAGMNGLAG PLHGLANQEV LVWLQKLRKE LGDNASEDKV KDFIWKTLKS GQVVPGYGHA VLRKTDPRYT CQREFALKHL PNDPLFQLVS NIYKVVPPIL TELGKVKNPW PNVDAHSGVL LQYYGLKEMN YYTVLFGVSR ALGVLASLVW DRALGLPIER PKSMSTDGLM KAVGAAK //