PCY1_CAEEL
ID PCY1_CAEEL Reviewed; 362 AA.
AC P49583;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Putative choline-phosphate cytidylyltransferase;
DE EC=2.7.7.15;
DE AltName: Full=CTP:phosphocholine cytidylyltransferase;
DE Short=CCT;
DE Short=CT;
DE AltName: Full=Phosphorylcholine transferase;
GN ORFNames=F08C6.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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;
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; FO080866; CCD67344.1; -; Genomic_DNA.
DR PIR; T15975; T15975.
DR RefSeq; NP_001033539.1; NM_001038450.2.
DR AlphaFoldDB; P49583; -.
DR SMR; P49583; -.
DR STRING; 6239.F08C6.2a; -.
DR iPTMnet; P49583; -.
DR EPD; P49583; -.
DR PaxDb; P49583; -.
DR PeptideAtlas; P49583; -.
DR EnsemblMetazoa; F08C6.2a.1; F08C6.2a.1; WBGene00017241.
DR GeneID; 181021; -.
DR KEGG; cel:CELE_F08C6.2; -.
DR UCSC; F08C6.2a; c. elegans.
DR CTD; 181021; -.
DR WormBase; F08C6.2a; CE30937; WBGene00017241; -.
DR eggNOG; KOG2804; Eukaryota.
DR HOGENOM; CLU_034585_4_1_1; -.
DR InParanoid; P49583; -.
DR OMA; RWPFSAK; -.
DR OrthoDB; 1172502at2759; -.
DR PhylomeDB; P49583; -.
DR Reactome; R-CEL-1483191; Synthesis of PC.
DR UniPathway; UPA00753; UER00739.
DR PRO; PR:P49583; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00017241; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; P49583; baseline and differential.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IDA:WormBase.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:WormBase.
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 3: Inferred from homology;
KW Lipid biosynthesis; Lipid metabolism; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..362
FT /note="Putative choline-phosphate cytidylyltransferase"
FT /id="PRO_0000208458"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..96
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172..173
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 200..204
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 41769 MW; E2845D72C326C199 CRC64;
MFIHKQEKMP QRKRTMDSPQ EEDVEVKKKA TEVEYVVRSL ASDEPAPFSD EALAITTREA
VDYSKKITLA MAEANEAGRP VRIYADGIYD LFHHGHANQL RQVKKMFPNV YLIVGVCGDR
DTHKYKGRTV TSEEERYDGV RHCRYVDEVY REAPWFCTVE FLKNLKVDFI AHDAIPYVAP
GEEDLYEKFR REGMFLETER TEGVSTSDVV CRIIRDYDKY VRRNLQRGYS PKELNVGFLA
ASKYQIQNKV DSLKSKGIEL LSTWKSKSDD IIRDFIDTFH KDGGLNAFGG RLKGIMSMSR
SPSPSPHEGS PTGIEHHLET QDEEEEEEAL EEEKVVEQKI VEKKEVVKKR SSRNKAKTPL
EY
