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CISY2_ARATH
ID   CISY2_ARATH             Reviewed;         514 AA.
AC   Q9LXS6; Q570I4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Citrate synthase 2, peroxisomal;
DE            EC=2.3.3.16;
DE   Flags: Precursor;
GN   Name=CSY2; OrderedLocusNames=At3g58750; ORFNames=T20N10.100;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 408-514.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=15923350; DOI=10.1105/tpc.105.031856;
RA   Pracharoenwattana I., Cornah J.E., Smith S.M.;
RT   "Arabidopsis peroxisomal citrate synthase is required for fatty acid
RT   respiration and seed germination.";
RL   Plant Cell 17:2037-2048(2005).
CC   -!- FUNCTION: Peroxisomal citrate synthase required for the fatty acid
CC       respiration in seedlings, citrate being exported from peroxisomes into
CC       mitochondria during respiration of triacylglycerol (TAG). Indeed,
CC       complete respiration requires the transfer of carbon in the form of
CC       citrate from the peroxisome to the mitochondria.
CC       {ECO:0000269|PubMed:15923350}.
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: Peroxisome {ECO:0000269|PubMed:15923350}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed throughout the shoot.
CC       Expressed in flower, silique, stem, cauline leaf, young leaf, mature
CC       leaf and senescent leaf. {ECO:0000269|PubMed:15923350}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout seedling growth.
CC       {ECO:0000269|PubMed:15923350}.
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=BAD93857.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL353032; CAB88292.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79826.1; -; Genomic_DNA.
DR   EMBL; BT015884; AAU95420.1; -; mRNA.
DR   EMBL; BT020195; AAV59261.1; -; mRNA.
DR   EMBL; AK220724; BAD93857.1; ALT_INIT; mRNA.
DR   PIR; T49158; T49158.
DR   RefSeq; NP_191434.1; NM_115737.3.
DR   AlphaFoldDB; Q9LXS6; -.
DR   SMR; Q9LXS6; -.
DR   BioGRID; 10359; 25.
DR   IntAct; Q9LXS6; 4.
DR   STRING; 3702.AT3G58750.1; -.
DR   iPTMnet; Q9LXS6; -.
DR   PaxDb; Q9LXS6; -.
DR   PRIDE; Q9LXS6; -.
DR   ProteomicsDB; 246695; -.
DR   EnsemblPlants; AT3G58750.1; AT3G58750.1; AT3G58750.
DR   GeneID; 825044; -.
DR   Gramene; AT3G58750.1; AT3G58750.1; AT3G58750.
DR   KEGG; ath:AT3G58750; -.
DR   Araport; AT3G58750; -.
DR   TAIR; locus:2098989; AT3G58750.
DR   eggNOG; KOG2617; Eukaryota.
DR   HOGENOM; CLU_025068_0_1_1; -.
DR   InParanoid; Q9LXS6; -.
DR   OMA; DRQLYPN; -.
DR   OrthoDB; 691172at2759; -.
DR   PhylomeDB; Q9LXS6; -.
DR   BioCyc; ARA:AT3G58750-MON; -.
DR   UniPathway; UPA00223; UER00717.
DR   PRO; PR:Q9LXS6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LXS6; baseline and differential.
DR   Genevisible; Q9LXS6; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IGI:TAIR.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IGI:TAIR.
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; 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   2: Evidence at transcript level;
KW   Peroxisome; Reference proteome; Transferase; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..?
FT                   /note="Peroxisome"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..514
FT                   /note="Citrate synthase 2, peroxisomal"
FT                   /id="PRO_0000005482"
FT   ACT_SITE        324
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   514 AA;  56603 MW;  1226E3B4AFF662B7 CRC64;
     MEISQRVKAR LAVLTAHLAV SDTVGLEQVL PAIAPWCTSA HITAAPHGSL KGNLTIVDER
     TGKKYQVPVS EHGTVKAVDL KKITTGKDDK GLKLYDPGYL NTAPVRSSIC YIDGDEGILR
     YRGYPIEELA ESSTFIEVAY LLMYGNLPSQ SQLADWEFTV SQHSAVPQGV LDIIQSMPHD
     AHPMGVLVSA MSALSIFHPD ANPALSGQDI YKSKQVRDKQ IVRILGKAPT IAAAAYLRTA
     GRPPVLPSAN LSYSENFLYM LDSMGNRSYK PNPRLARVLD ILFILHAEHE MNCSTAAARH
     LASSGVDVYT ACAGAVGALY GPLHGGANEA VLKMLAEIGT AENIPDFIEG VKNRKRKMSG
     FGHRVYKNYD PRAKVIKKLA DEVFSIVGRD PLIEVAVALE KAALSDEYFV KRKLYPNVDF
     YSGLIYRAMG FPPEFFTVLF AVPRMAGYLS HWRESLDDPD TRIMRPQQAY TGVWMRHYEP
     VRERTLSSDS DKDKFGQVSI SNASRRRLAG SSAL
 
 
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