CISY5_ARATH
ID CISY5_ARATH Reviewed; 464 AA.
AC Q9M1D3; F4JAL9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Citrate synthase 5, mitochondrial;
DE EC=2.3.3.16;
DE Flags: Precursor;
GN Name=CSY5; OrderedLocusNames=At3g60100; ORFNames=T2O9.80;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
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=2.3.3.16; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10117};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14671022}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB75925.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL138658; CAB75925.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80011.1; -; Genomic_DNA.
DR PIR; T47834; T47834.
DR RefSeq; NP_191569.2; NM_115873.3.
DR AlphaFoldDB; Q9M1D3; -.
DR SMR; Q9M1D3; -.
DR BioGRID; 10494; 19.
DR STRING; 3702.AT3G60100.1; -.
DR PaxDb; Q9M1D3; -.
DR PRIDE; Q9M1D3; -.
DR ProteomicsDB; 246802; -.
DR EnsemblPlants; AT3G60100.1; AT3G60100.1; AT3G60100.
DR GeneID; 825180; -.
DR Gramene; AT3G60100.1; AT3G60100.1; AT3G60100.
DR KEGG; ath:AT3G60100; -.
DR Araport; AT3G60100; -.
DR TAIR; locus:2101467; AT3G60100.
DR eggNOG; KOG2617; Eukaryota.
DR HOGENOM; CLU_022049_2_1_1; -.
DR InParanoid; Q9M1D3; -.
DR UniPathway; UPA00223; UER00717.
DR PRO; PR:Q9M1D3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1D3; baseline and differential.
DR Genevisible; Q9M1D3; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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 Mitochondrion; Reference proteome; Transferase; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..464
FT /note="Citrate synthase 5, mitochondrial"
FT /id="PRO_0000005485"
FT ACT_SITE 300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ SEQUENCE 464 AA; 51724 MW; 2D2AE88A6AA29BB2 CRC64;
MVFFRSVSAI SRLRSRAVQQ SSLSNSVRWL HSSELDLKSQ MQEIIPEQQD RLKKLKSEQG
KVPVGNITVD MVLGGMRGMT GLLWETSLLD ADEGIRFRGM SIPECQKILP SAESGEEPLP
ESLLWLLLTG KVPTKEQANA LSTELAHRAA VPAIDALPST AHPMTQFASG VMALQVQSEF
QKAYEQGDIS KSKYWEPTFE DALNLIARVP VVASYVYRRM YKDGSIIPLD DSLDYGANFS
HMLGFDSPQM KELMRLYVTI HSDHEGGNVS AHAGHLVGSA LSDPYLSFAA ALNGLAGPLH
GLANQEVLLW IKLVVEECGE SISKEQLKDY VWKTLNSGKV VPGYGHGVLR KTDPRYICQR
EFALKHLPDD PLFQLVSKLY EVVPPILTEL GKVKNPWPNV DAHSGVLLNY YGLTEARYYT
VLFGVSRSLG ICSQLIWDRA LGLPLERPKS VNMDWLDNFT RLNR
