CISY4_ARATH
ID CISY4_ARATH Reviewed; 474 AA.
AC P20115; O64869; Q8LE36; Q94EY6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Citrate synthase 4, mitochondrial;
DE EC=2.3.3.16;
DE Flags: Precursor;
GN Name=CSY4; OrderedLocusNames=At2g44350; ORFNames=F4I1.16;
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 [MRNA] (ISOFORM 1).
RX PubMed=2491664; DOI=10.1007/bf00015553;
RA Unger E.A., Hand J.M., Cashmore A.R., Vasconcelos A.C.;
RT "Isolation of a cDNA encoding mitochondrial citrate synthase from
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 13:411-418(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND POSSIBLE SUBCELLULAR LOCATION.
RX PubMed=15157177; DOI=10.1042/bst0320524;
RA Slabas A.R., Ndimba B., Simon W.J., Chivasa S.;
RT "Proteomic analysis of the Arabidopsis cell wall reveals unexpected
RT proteins with new cellular locations.";
RL Biochem. Soc. Trans. 32:524-528(2004).
RN [7]
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 -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14671022}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P20115-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P20115-2; Sequence=VSP_009185;
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=CAA35570.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X17528; CAA35570.1; ALT_FRAME; mRNA.
DR EMBL; AC004521; AAC16084.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10410.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10411.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62353.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62354.1; -; Genomic_DNA.
DR EMBL; AF387018; AAK62463.1; -; mRNA.
DR EMBL; BT006613; AAP31957.1; -; mRNA.
DR EMBL; AY085647; AAM62868.1; -; mRNA.
DR PIR; JA0149; YKMUM.
DR PIR; T02390; T02390.
DR RefSeq; NP_001324514.1; NM_001337082.1. [P20115-1]
DR RefSeq; NP_001324515.1; NM_001337083.1. [P20115-2]
DR RefSeq; NP_566016.1; NM_129998.3. [P20115-2]
DR RefSeq; NP_850415.1; NM_180084.2. [P20115-1]
DR PDB; 6K5V; X-ray; 2.69 A; A/B/C/D/E/F=17-474.
DR PDBsum; 6K5V; -.
DR AlphaFoldDB; P20115; -.
DR SMR; P20115; -.
DR BioGRID; 4378; 25.
DR IntAct; P20115; 2.
DR STRING; 3702.AT2G44350.2; -.
DR PaxDb; P20115; -.
DR PRIDE; P20115; -.
DR ProteomicsDB; 246696; -. [P20115-1]
DR EnsemblPlants; AT2G44350.1; AT2G44350.1; AT2G44350. [P20115-2]
DR EnsemblPlants; AT2G44350.2; AT2G44350.2; AT2G44350. [P20115-1]
DR EnsemblPlants; AT2G44350.3; AT2G44350.3; AT2G44350. [P20115-1]
DR EnsemblPlants; AT2G44350.4; AT2G44350.4; AT2G44350. [P20115-2]
DR GeneID; 819042; -.
DR Gramene; AT2G44350.1; AT2G44350.1; AT2G44350. [P20115-2]
DR Gramene; AT2G44350.2; AT2G44350.2; AT2G44350. [P20115-1]
DR Gramene; AT2G44350.3; AT2G44350.3; AT2G44350. [P20115-1]
DR Gramene; AT2G44350.4; AT2G44350.4; AT2G44350. [P20115-2]
DR KEGG; ath:AT2G44350; -.
DR Araport; AT2G44350; -.
DR TAIR; locus:2050554; AT2G44350.
DR eggNOG; KOG2617; Eukaryota.
DR InParanoid; P20115; -.
DR OMA; ELIRHEW; -.
DR OrthoDB; 1131452at2759; -.
DR PhylomeDB; P20115; -.
DR BioCyc; ARA:AT2G44350-MON; -.
DR BioCyc; MetaCyc:AT2G44350-MON; -.
DR BRENDA; 2.3.3.16; 399.
DR UniPathway; UPA00223; UER00717.
DR PRO; PR:P20115; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P20115; baseline and differential.
DR Genevisible; P20115; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
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 3D-structure; Alternative splicing; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..474
FT /note="Citrate synthase 4, mitochondrial"
FT /id="PRO_0000005484"
FT ACT_SITE 308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT VAR_SEQ 18
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.5"
FT /id="VSP_009185"
FT CONFLICT 25
FT /note="S -> N (in Ref. 5; AAM62868)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..53
FT /note="QQ -> HK (in Ref. 1; CAA35570)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="V -> AL (in Ref. 1; CAA35570)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="P -> S (in Ref. 1; CAA35570)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..258
FT /note="KV -> RL (in Ref. 1; CAA35570)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="L -> H (in Ref. 1; CAA35570)"
FT /evidence="ECO:0000305"
FT CONFLICT 383..385
FT /note="LVS -> CC (in Ref. 1; CAA35570)"
FT /evidence="ECO:0000305"
FT CONFLICT 448..450
FT /note="ALG -> ELL (in Ref. 1; CAA35570)"
FT /evidence="ECO:0000305"
FT HELIX 41..63
FT /evidence="ECO:0007829|PDB:6K5V"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:6K5V"
FT TURN 78..82
FT /evidence="ECO:0007829|PDB:6K5V"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6K5V"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6K5V"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:6K5V"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 203..229
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 292..303
FT /evidence="ECO:0007829|PDB:6K5V"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 311..326
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:6K5V"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 379..398
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 412..418
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 427..448
FT /evidence="ECO:0007829|PDB:6K5V"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:6K5V"
FT HELIX 461..468
FT /evidence="ECO:0007829|PDB:6K5V"
SQ SEQUENCE 474 AA; 52782 MW; D306BD540868FCA9 CRC64;
MVFFRSVSAF TRLRSRVQGQ QSSLSNSVRW IQMQSSTDLD LKSQLQELIP EQQDRLKKLK
SEHGKVQLGN ITVDMVIGGM RGMTGLLWET SLLDPEEGIR FRGLSIPECQ KVLPTAQSGA
EPLPEGLLWL LLTGKVPSKE QVEALSKDLA NRAAVPDYVY NAIDALPSTA HPMTQFASGV
MALQVQSEFQ KAYENGIHKS KFWEPTYEDC LNLIARVPVV AAYVYRRMYK NGDSIPSDKS
LDYGANFSHM LGFDDEKVKE LMRLYITIHS DHEGGNVSAH TGHLVGSALS DPYLSFAAAL
NGLAGPLHGL ANQEVLLWIK SVVEECGEDI SKEQLKEYVW KTLNSGKVIP GYGHGVLRNT
DPRYVCQREF ALKHLPDDPL FQLVSKLYEV VPPVLTELGK VKNPWPNVDA HSGVLLNHYG
LTEARYYTVL FGVSRSLGIC SQLIWDRALG LALERPKSVT MDWLEAHCKK ASSA
