CISY_BOVIN
ID CISY_BOVIN Reviewed; 466 AA.
AC Q29RK1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Citrate synthase, mitochondrial;
DE EC=2.3.3.1;
DE AltName: Full=Citrate (Si)-synthase;
DE Flags: Precursor;
GN Name=CS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP ACETYLATION AT LYS-76, AND SUCCINYLATION AT LYS-76.
RX PubMed=22076378; DOI=10.1126/science.1207861;
RA Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J.,
RA Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J.,
RA Hao Q., Lin H.;
RT "Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase.";
RL Science 334:806-809(2011).
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; BC114138; AAI14139.1; -; mRNA.
DR RefSeq; NP_001038186.1; NM_001044721.1.
DR AlphaFoldDB; Q29RK1; -.
DR SMR; Q29RK1; -.
DR IntAct; Q29RK1; 1.
DR STRING; 9913.ENSBTAP00000005730; -.
DR ChEMBL; CHEMBL2406901; -.
DR iPTMnet; Q29RK1; -.
DR PaxDb; Q29RK1; -.
DR PeptideAtlas; Q29RK1; -.
DR PRIDE; Q29RK1; -.
DR Ensembl; ENSBTAT00000005730; ENSBTAP00000005730; ENSBTAG00000004371.
DR GeneID; 280682; -.
DR KEGG; bta:280682; -.
DR CTD; 1431; -.
DR VEuPathDB; HostDB:ENSBTAG00000004371; -.
DR VGNC; VGNC:27748; CS.
DR eggNOG; KOG2617; Eukaryota.
DR GeneTree; ENSGT00390000006813; -.
DR HOGENOM; CLU_022049_2_1_1; -.
DR InParanoid; Q29RK1; -.
DR OMA; TVGWCAQ; -.
DR OrthoDB; 1131452at2759; -.
DR TreeFam; TF300398; -.
DR Reactome; R-BTA-71403; Citric acid cycle (TCA cycle).
DR SABIO-RK; Q29RK1; -.
DR UniPathway; UPA00223; UER00717.
DR PRO; PR:Q29RK1; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000004371; Expressed in oocyte and 106 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Methylation; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transferase; 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_0000244377"
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:0000269|PubMed:22076378"
FT MOD_RES 76
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22076378"
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 226
FT /note="Phosphoserine"
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; 51773 MW; 73C2CB93589084B3 CRC64;
MALLTAAARL FGAKNASCLV LAARHASASS TNLKDILADL IPKEQTRVKA FRQQHGKTVV
GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE CQKLLPKAKG GEEPLPEGLF
WLLVTGQIPT EEQVSWLSQE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AVTALNSEST
FARAYSEGIN RTKYWELIYE DSMDLIAKLP CVAAKIYRNL YREGSSIGAI DPKLDWSHNF
TNMLGYTDAQ FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL RKTDPRYTCQ
REFALKHLPQ DPMFKLVAQL YKIVPNILLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY
TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTDGLMKF VDSKSG
