PCY2_DICDI
ID PCY2_DICDI Reviewed; 360 AA.
AC Q55BZ4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ethanolamine-phosphate cytidylyltransferase;
DE EC=2.7.7.14 {ECO:0000250|UniProtKB:Q99447};
DE AltName: Full=CTP:phosphoethanolamine cytidylyltransferase;
DE AltName: Full=Phosphorylethanolamine transferase;
GN Name=pctA; ORFNames=DDB_G0270298;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
CC -!- FUNCTION: Ethanolamine-phosphate cytidylyltransferase that catalyzes
CC the second step in the synthesis of phosphatidylethanolamine (PE) from
CC ethanolamine via the CDP-ethanolamine pathway.
CC {ECO:0000250|UniProtKB:Q99447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphoethanolamine = CDP-ethanolamine +
CC diphosphate; Xref=Rhea:RHEA:24592, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57876,
CC ChEBI:CHEBI:58190; EC=2.7.7.14;
CC Evidence={ECO:0000250|UniProtKB:Q99447};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24593;
CC Evidence={ECO:0000250|UniProtKB:Q99447};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
CC {ECO:0000250|UniProtKB:Q99447}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72499.1; -; Genomic_DNA.
DR RefSeq; XP_646687.1; XM_641595.1.
DR AlphaFoldDB; Q55BZ4; -.
DR SMR; Q55BZ4; -.
DR STRING; 44689.DDB0191331; -.
DR PaxDb; Q55BZ4; -.
DR EnsemblProtists; EAL72499; EAL72499; DDB_G0270298.
DR GeneID; 8617662; -.
DR KEGG; ddi:DDB_G0270298; -.
DR dictyBase; DDB_G0270298; pctA.
DR eggNOG; KOG2803; Eukaryota.
DR HOGENOM; CLU_031246_2_2_1; -.
DR InParanoid; Q55BZ4; -.
DR OMA; VLQCKYI; -.
DR PhylomeDB; Q55BZ4; -.
DR Reactome; R-DDI-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00742.
DR PRO; PR:Q55BZ4; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0004306; F:ethanolamine-phosphate cytidylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISS:dictyBase.
DR CDD; cd02174; CCT; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR044608; Ect1/PCYT2.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR45780; PTHR45780; 1.
DR Pfam; PF01467; CTP_transf_like; 2.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 2.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..360
FT /note="Ethanolamine-phosphate cytidylyltransferase"
FT /id="PRO_0000327721"
FT BINDING 207..208
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 215..218
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 291..294
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 321..325
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
SQ SEQUENCE 360 AA; 40301 MW; BD698DE154E1ECBB CRC64;
MSTTTNKKPI RVYVDGCFDL MHFGHANALR QARELGDILV VGVHTDEEIA KNKGPPVMNE
QERYKAVRAC KWADEVAEGA PYTLTEEYLD SLNCDFCVHG EDISVGADGK DVYEGIKKSG
KFRFIKRTEG VSTTELVGRM LLCTKDHLQN VSGEQTSPLG GVNPNVLHKQ SPYTSLSHFL
PTTRKIVQFS EGRSPKPNDK IIYMDGGFDL FHVGHTEALK QARALGDYLI VGVHDDRVVH
EQKGSNFPIM NLHERVLSVL SCRYVDEVVI GAPFSVTKDM IDSLHINVVV HGDDQVVLGP
EGGVDPYKLP RELGIYKEVK HTEGLTATEI VKRIIDNRLQ YEARNRKKEA KEINFIEQSN
