CISY2_AEDAE
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 25-MAY-2022, entry version 96.
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}.
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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.AAEL011789-PB; -.
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; TVGWCAQ; -.
DR OrthoDB; 1131452at2759; -.
DR PhylomeDB; Q16P20; -.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000008820; Chromosome 3.
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 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