CISY_MESAU
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 25-MAY-2022, entry version 58.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ403127; ABD77260.1; -; mRNA.
DR AlphaFoldDB; Q0QEL7; -.
DR SMR; Q0QEL7; -.
DR STRING; 10036.XP_005079779.1; -.
DR PRIDE; Q0QEL7; -.
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; 1.10.230.10; -; 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; 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 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
