ID   CISY1_AEDAE             Reviewed;         467 AA.
AC   Q17GM7;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Probable citrate synthase 1, mitochondrial;
DE            EC=2.3.3.16;
DE   Flags: Precursor;
GN   ORFNames=AAEL002956;
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}.
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DR   EMBL; CH477258; EAT45772.1; -; Genomic_DNA.
DR   RefSeq; XP_001656210.1; XM_001656160.1.
DR   AlphaFoldDB; Q17GM7; -.
DR   SMR; Q17GM7; -.
DR   STRING; 7159.AAEL002956-PA; -.
DR   VEuPathDB; VectorBase:AAEL011789; -.
DR   eggNOG; KOG2617; Eukaryota.
DR   HOGENOM; CLU_022049_2_1_1; -.
DR   InParanoid; Q17GM7; -.
DR   OMA; NEAVMHM; -.
DR   PhylomeDB; Q17GM7; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000008820; 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   Gene3D; 1.10.230.10; -; 1.
DR   Gene3D; 1.10.580.10; -; 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   PANTHER; PTHR11739; PTHR11739; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; SSF48256; 1.
DR   TIGRFAMs; TIGR01793; cit_synth_euk; 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 1, mitochondrial"
FT                   /id="PRO_0000291601"
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;  51657 MW;  4033D11312107CB9 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 KAVGASK