CCT1_ARATH
ID CCT1_ARATH Reviewed; 332 AA.
AC Q9ZV56;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Choline-phosphate cytidylyltransferase 1 {ECO:0000303|PubMed:12461134};
DE Short=AtCCT1 {ECO:0000303|PubMed:12461134};
DE EC=2.7.7.15 {ECO:0000269|PubMed:12461134};
DE AltName: Full=CTP:phosphocholine cytidylyltransferase 1 {ECO:0000305};
DE AltName: Full=Phosphorylcholine transferase 1 {ECO:0000305};
GN Name=CCT1 {ECO:0000303|PubMed:12461134}; Synonyms=CCT {ECO:0000303|Ref.1};
GN OrderedLocusNames=At2g32260 {ECO:0000312|Araport:AT2G32260};
GN ORFNames=T32F6.22 {ECO:0000312|EMBL:AAC69950.1};
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Choi Y.H., Choi S.B., Cho S.H.;
RT "Structure of a CTP:phosphocholine cytidylyltransferase gene from
RT Arabidopsis thaliana.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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].
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 BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12461134; DOI=10.1093/pcp/pcf169;
RA Inatsugi R., Nakamura M., Nishida I.;
RT "Phosphatidylcholine biosynthesis at low temperature: differential
RT expression of CTP:phosphorylcholine cytidylyltransferase isogenes in
RT Arabidopsis thaliana.";
RL Plant Cell Physiol. 43:1342-1350(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19667100; DOI=10.1093/pcp/pcp115;
RA Inatsugi R., Kawai H., Yamaoka Y., Yu Y., Sekiguchi A., Nakamura M.,
RA Nishida I.;
RT "Isozyme-specific modes of activation of CTP:phosphorylcholine
RT cytidylyltransferase in Arabidopsis thaliana at low temperature.";
RL Plant Cell Physiol. 50:1727-1735(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Plays an important role in the biosynthesis of the
CC phospholipid phosphatidylcholine. Catalyzes the formation of CDP-
CC choline. {ECO:0000269|PubMed:19667100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate;
CC Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975;
CC EC=2.7.7.15; Evidence={ECO:0000269|PubMed:19667100};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998;
CC Evidence={ECO:0000269|PubMed:19667100};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:12461134};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19667100}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; AF165912; AAD45922.1; -; Genomic_DNA.
DR EMBL; AC005700; AAC69950.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08659.1; -; Genomic_DNA.
DR EMBL; AY136393; AAM97059.1; -; mRNA.
DR EMBL; BT000207; AAN15526.1; -; mRNA.
DR PIR; H84730; H84730.
DR RefSeq; NP_180785.1; NM_128785.3.
DR AlphaFoldDB; Q9ZV56; -.
DR SMR; Q9ZV56; -.
DR STRING; 3702.AT2G32260.1; -.
DR iPTMnet; Q9ZV56; -.
DR PaxDb; Q9ZV56; -.
DR PRIDE; Q9ZV56; -.
DR ProteomicsDB; 223906; -.
DR EnsemblPlants; AT2G32260.1; AT2G32260.1; AT2G32260.
DR GeneID; 817786; -.
DR Gramene; AT2G32260.1; AT2G32260.1; AT2G32260.
DR KEGG; ath:AT2G32260; -.
DR Araport; AT2G32260; -.
DR TAIR; locus:2062591; AT2G32260.
DR eggNOG; KOG2804; Eukaryota.
DR HOGENOM; CLU_034585_1_0_1; -.
DR InParanoid; Q9ZV56; -.
DR OMA; WVISREF; -.
DR OrthoDB; 1172502at2759; -.
DR PhylomeDB; Q9ZV56; -.
DR BioCyc; ARA:AT2G32260-MON; -.
DR BRENDA; 2.7.7.15; 399.
DR UniPathway; UPA00753; UER00739.
DR PRO; PR:Q9ZV56; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZV56; baseline and differential.
DR Genevisible; Q9ZV56; AT.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IMP:TAIR.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IMP:TAIR.
DR CDD; cd02174; CCT; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR045049; Pcy1-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR10739; PTHR10739; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW Acetylation; Lipid biosynthesis; Lipid metabolism; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..332
FT /note="Choline-phosphate cytidylyltransferase 1"
FT /id="PRO_0000423342"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..318
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..50
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 81
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 127..128
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 132
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT BINDING 157..161
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:P19836"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 332 AA; 38486 MW; 536E2FB87907AB54 CRC64;
MSNVIGDRTE DGLSTAAAAS GSTAVQSSPP TDRPVRVYAD GIYDLFHFGH ARSLEQAKLA
FPNNTYLLVG CCNDETTHKY KGRTVMTAEE RYESLRHCKW VDEVIPDAPW VVNQEFLDKH
QIDYVAHDSL PYADSSGAGK DVYEFVKKVG RFKETQRTEG ISTSDIIMRI VKDYNQYVMR
NLDRGYSRED LGVSFVKEKR LRVNMRLKKL QERVKEQQER VGEKIQTVKM LRNEWVENAD
RWVAGFLEIF EEGCHKMGTA IVDSIQERLM RQKSAERLEN GQDDDTDDQF YEEYFDHDMG
SDDDEDEKFY DEEEVKEEET EKTVMTDAKD NK
