CISY_MACFA
ID CISY_MACFA Reviewed; 466 AA.
AC P0C1Z2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Citrate synthase, mitochondrial;
DE EC=2.3.3.1;
DE AltName: Full=Citrate (Si)-synthase;
DE Flags: Precursor;
GN Name=CS; ORFNames=QtrA-16253;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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=2.3.3.1; 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 -!- PTM: Methylated. Trimethylation at Lys-395 by CSKMT decreases citrate
CC synthase activity. {ECO:0000250|UniProtKB:O75390}.
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; AB174355; BAE91417.1; -; mRNA.
DR RefSeq; NP_001272053.1; NM_001285124.1.
DR AlphaFoldDB; P0C1Z2; -.
DR SMR; P0C1Z2; -.
DR STRING; 9541.XP_005571273.1; -.
DR GeneID; 101926620; -.
DR CTD; 1431; -.
DR eggNOG; KOG2617; Eukaryota.
DR OrthoDB; 1131452at2759; -.
DR UniPathway; UPA00223; UER00717.
DR Proteomes; UP000233100; Unplaced.
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 2: Evidence at transcript level;
KW Acetylation; Methylation; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 28..466
FT /note="Citrate synthase, mitochondrial"
FT /id="PRO_0000235795"
FT ACT_SITE 301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 76
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q29RK1"
FT MOD_RES 76
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q29RK1"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 193
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 321
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 321
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 327
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75390"
FT MOD_RES 327
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 375
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75390"
FT MOD_RES 375
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 382
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75390"
FT MOD_RES 393
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75390"
FT MOD_RES 393
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 395
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75390"
FT MOD_RES 450
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 459
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 459
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
SQ SEQUENCE 466 AA; 51698 MW; EFECCDC06EAC4E00 CRC64;
MALLTAAARL LGTKNASCLV LAARHASASS TNLKDILADL IPKEQARIKT FRQQHGKTVV
GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGFSIPE CQKLLPKAKG GEEPLPEGLF
WLLVTGQIPT EEQVSWLSKE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AVTALNSESN
FARAYAEGIS RTKYWELIYE DSMDLIAKLP CIAAKIYRNL YREGSGIGAI DSNLDWSHNF
TNMLGYTDSQ FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL RKTDPRYTCQ
REFALKHLPN DPMFKLVAQL YKIVPNVLLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY
TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTEGLMKF VDSKSG
