CISY_DANRE
ID CISY_DANRE Reviewed; 468 AA.
AC Q7ZVY5;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=zgc:55507;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) 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 -!- 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; BC045362; AAH45362.1; -; mRNA.
DR RefSeq; NP_955892.1; NM_199598.1.
DR AlphaFoldDB; Q7ZVY5; -.
DR SMR; Q7ZVY5; -.
DR STRING; 7955.ENSDARP00000094021; -.
DR PaxDb; Q7ZVY5; -.
DR PRIDE; Q7ZVY5; -.
DR GeneID; 322339; -.
DR KEGG; dre:322339; -.
DR CTD; 1431; -.
DR ZFIN; ZDB-GENE-030131-1058; cs.
DR eggNOG; KOG2617; Eukaryota.
DR InParanoid; Q7ZVY5; -.
DR OrthoDB; 1131452at2759; -.
DR PhylomeDB; Q7ZVY5; -.
DR Reactome; R-DRE-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00717.
DR PRO; PR:Q7ZVY5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:0014823; P:response to activity; IDA:ZFIN.
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 2: Evidence at transcript level;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 31..468
FT /note="Citrate synthase, mitochondrial"
FT /id="PRO_0000253902"
FT ACT_SITE 303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ SEQUENCE 468 AA; 51751 MW; 81F3D0260317065F CRC64;
MSFLSISRLA PRLLSSKNAA CVVVAARNAS ASTNLKDVLS DLVPKEQSRI KNFKQQYGKT
SIGQITVDMV YGGMRGVKGL VYETSVLDPD EGIRFRGYSI PECQQLLPKA PGGEEPLPEG
LFWLLVTGQV PTEEQVSWLS KEWAKRAALP SHVVTMLDNF PTNLHPMSQF SAAITALNSE
SSFARAYSEG VNKAKYWEFV YEDSMDLIAK LPCVAAKIYR NLYREGSSIG AIDSNLDWSH
NFTNMLGYTE PQFTELMRLY LTIHSDHEGG NVSAHTSHLV GSALSDPYLS FSAAMNGLAG
PLHGLANQEV LVWLTALQKE LGGEVSDEKM RDYIWNTLKS GRVVPGYGHA VLRKTDPRYT
CQREFALKHL PNDPMFKLVA QLYKIVPNVL LEQGKAKNPW PNVDAHSGVL LQYYGMTEMN
YYTVLFGVSR ALGVLAQLVW SRALGFPLER PKSMSTDGLM ALVGAKSG