ID   CISY_MESAU              Reviewed;         213 AA.
AC   Q0QEL7; P86224;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Citrate synthase, mitochondrial {ECO:0000250|UniProtKB:P00889};
DE            EC=2.3.3.1;
DE   AltName: Full=Citrate (Si)-synthase;
DE   Flags: Fragment;
GN   Name=CS {ECO:0000312|EMBL:ABD77260.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1] {ECO:0000312|EMBL:ABD77260.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver {ECO:0000312|EMBL:ABD77260.1};
RX   PubMed=16751257; DOI=10.1093/molbev/msl027;
RA   Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT   "Housekeeping genes for phylogenetic analysis of eutherian relationships.";
RL   Mol. Biol. Evol. 23:1493-1503(2006).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
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;
CC         Evidence={ECO:0000250|UniProtKB:P00889, ECO:0000255|PROSITE-
CC         ProRule:PRU10117};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 1/2. {ECO:0000250|UniProtKB:P00889}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00889}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P00889}.
CC   -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC       oxidative metabolism. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000255}.
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DR   EMBL; DQ403127; ABD77260.1; -; mRNA.
DR   AlphaFoldDB; Q0QEL7; -.
DR   SMR; Q0QEL7; -.
DR   STRING; 10036.ENSMAUP00000023353; -.
DR   eggNOG; KOG2617; Eukaryota.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR   Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 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; IPR036969; Citrate_synthase_sf.
DR   PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR11739:SF8; CITRATE SYNTHASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; Citrate synthase; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Methylation; Mitochondrion; Reference proteome; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           <1..>213
FT                   /note="Citrate synthase, mitochondrial"
FT                   /id="PRO_0000394310"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000250|UniProtKB:P00889,
FT                   ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000250|UniProtKB:P00889,
FT                   ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000250|UniProtKB:P00889,
FT                   ECO:0000255|PROSITE-ProRule:PRU10117"
FT   MOD_RES         94
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT   MOD_RES         94
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT   MOD_RES         100
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O75390"
FT   MOD_RES         100
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT   MOD_RES         148
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O75390"
FT   MOD_RES         148
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT   MOD_RES         155
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O75390"
FT   MOD_RES         166
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O75390"
FT   MOD_RES         166
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT   MOD_RES         168
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O75390"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ABD77260.1"
FT   NON_TER         213
FT                   /evidence="ECO:0000312|EMBL:ABD77260.1"
SQ   SEQUENCE   213 AA;  23884 MW;  F423CBF73DF89D63 CRC64;
     GAIDSKLDWS HNFTNMLGYT EPQFTELMRL YLTIHSDHEG GNVSAHTSHL VGSALSDPYL
     SFAAAMNGLA GPLHGLANQE VLVWLTQLQK EVGKDVSDEK LRDYIWNTLN SGRVVPGYGH
     AVLRKTDPRY SCQREFALKH LPNDPLFKLV AQLYKIVPNI LLEQGKAKNP WPNVDAHSGV
     LLQYYGMTEM NYYTVLFGVS RALGVLAQLI WSR
//