CISY_PIG
ID CISY_PIG Reviewed; 464 AA.
AC P00889;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 153.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3048387; DOI=10.1021/bi00413a015;
RA Evans C.T., Owens D.D., Sumegi B., Kispal G., Srere P.A.;
RT "Isolation, nucleotide sequence, and expression of a cDNA encoding pig
RT citrate synthase.";
RL Biochemistry 27:4680-4686(1988).
RN [2]
RP PROTEIN SEQUENCE OF 28-464, AND METHYLATION AT LYS-395.
RX PubMed=7093227; DOI=10.1021/bi00538a009;
RA Bloxham D.P., Parmelee D.C., Kumar S., Walsh K.A., Titani K.;
RT "Complete amino acid sequence of porcine heart citrate synthase.";
RL Biochemistry 21:2028-2036(1982).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=7120407; DOI=10.1016/0022-2836(82)90452-1;
RA Remington S., Wiegand G., Huber R.;
RT "Crystallographic refinement and atomic models of two different forms of
RT citrate synthase at 2.7- and 1.7-A resolution.";
RL J. Mol. Biol. 158:111-152(1982).
RN [4]
RP MUTAGENESIS.
RX PubMed=1702991; DOI=10.1021/bi00485a003;
RA Alter G.M., Casazza J.P., Zhi W., Nemeth P., Srere P.A., Evans C.T.;
RT "Mutation of essential catalytic residues in pig citrate synthase.";
RL Biochemistry 29:7557-7563(1990).
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- PTM: Methylated (PubMed:7093227). Trimethylation at Lys-395 by CSKMT
CC decreases citrate synthase activity (By similarity).
CC {ECO:0000250|UniProtKB:O75390, ECO:0000269|PubMed:7093227}.
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; M21197; AAA31017.1; -; mRNA.
DR PIR; A29966; YKPG.
DR RefSeq; NP_999441.1; NM_214276.1.
DR PDB; 1CTS; X-ray; 2.70 A; A=28-464.
DR PDB; 2CTS; X-ray; 2.00 A; A=28-464.
DR PDB; 3ENJ; X-ray; 1.78 A; A=28-464.
DR PDB; 4CTS; X-ray; 2.90 A; A/B=28-464.
DR PDB; 5UQS; X-ray; 1.60 A; A/C=1-464.
DR PDBsum; 1CTS; -.
DR PDBsum; 2CTS; -.
DR PDBsum; 3ENJ; -.
DR PDBsum; 4CTS; -.
DR PDBsum; 5UQS; -.
DR AlphaFoldDB; P00889; -.
DR PCDDB; P00889; -.
DR SMR; P00889; -.
DR BioGRID; 1149646; 2.
DR STRING; 9823.ENSSSCP00000021332; -.
DR iPTMnet; P00889; -.
DR PaxDb; P00889; -.
DR PeptideAtlas; P00889; -.
DR PRIDE; P00889; -.
DR Ensembl; ENSSSCT00000045632; ENSSSCP00000056310; ENSSSCG00000035686.
DR Ensembl; ENSSSCT00005038623; ENSSSCP00005023708; ENSSSCG00005024394.
DR Ensembl; ENSSSCT00005038710; ENSSSCP00005023775; ENSSSCG00005024394.
DR Ensembl; ENSSSCT00015100520; ENSSSCP00015041581; ENSSSCG00015074449.
DR Ensembl; ENSSSCT00070059648; ENSSSCP00070050810; ENSSSCG00070029675.
DR GeneID; 397519; -.
DR KEGG; ssc:397519; -.
DR CTD; 1431; -.
DR VGNC; VGNC:103225; CS.
DR eggNOG; KOG2617; Eukaryota.
DR GeneTree; ENSGT00390000006813; -.
DR HOGENOM; CLU_087652_0_0_1; -.
DR InParanoid; P00889; -.
DR OrthoDB; 1131452at2759; -.
DR BRENDA; 2.3.3.1; 6170.
DR BRENDA; 2.3.3.16; 6170.
DR Reactome; R-SSC-71403; Citric acid cycle (TCA cycle).
DR SABIO-RK; P00889; -.
DR UniPathway; UPA00223; UER00717.
DR EvolutionaryTrace; P00889; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Proteomes; UP000314985; Chromosome 5.
DR Bgee; ENSSSCG00000035686; Expressed in psoas major muscle and 42 other tissues.
DR ExpressionAtlas; P00889; baseline and differential.
DR Genevisible; P00889; SS.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; ISS:UniProtKB.
DR GO; GO:0036440; F:citrate synthase activity; IDA:CAFA.
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; 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 3D-structure; Acetylation; Direct protein sequencing; Methylation;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transferase;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7093227"
FT CHAIN 28..464
FT /note="Citrate synthase, mitochondrial"
FT /id="PRO_0000005473"
FT ACT_SITE 301
FT ACT_SITE 347
FT ACT_SITE 402
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 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:0000269|PubMed:7093227"
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"
FT HELIX 33..55
FT /evidence="ECO:0007829|PDB:5UQS"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:5UQS"
FT TURN 70..74
FT /evidence="ECO:0007829|PDB:5UQS"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:5UQS"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5UQS"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5UQS"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:5UQS"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4CTS"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2CTS"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:5UQS"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2CTS"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 194..221
FT /evidence="ECO:0007829|PDB:5UQS"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1CTS"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:5UQS"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:2CTS"
FT HELIX 270..280
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 304..319
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 325..337
FT /evidence="ECO:0007829|PDB:5UQS"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:3ENJ"
FT HELIX 355..367
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 372..391
FT /evidence="ECO:0007829|PDB:5UQS"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:3ENJ"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 420..441
FT /evidence="ECO:0007829|PDB:5UQS"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:5UQS"
FT HELIX 454..463
FT /evidence="ECO:0007829|PDB:5UQS"
SQ SEQUENCE 464 AA; 51629 MW; 66719A7504DF322A CRC64;
MALLTAAARL FGAKNASCLV LAARHASASS TNLKDILADL IPKEQARIKT FRQQHGNTVV
GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE CQKMLPKAKG GEEPLPEGLF
WLLVTGQIPT EEQVSWLSKE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AITALNSESN
FARAYAEGIH RTKYWELIYE DCMDLIAKLP CVAAKIYRNL YREGSSIGAI DSKLDWSHNF
TNMLGYTDAQ FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL RKTDPRYTCQ
REFALKHLPH DPMFKLVAQL YKIVPNVLLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY
TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTDGLIKL VDSK
