ECT1_SCHPO
ID ECT1_SCHPO Reviewed; 365 AA.
AC Q9UTI6; P78849;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable ethanolamine-phosphate cytidylyltransferase;
DE EC=2.7.7.14;
DE AltName: Full=CTP:phosphoethanolamine cytidylyltransferase;
DE AltName: Full=Phosphorylethanolamine transferase;
GN ORFNames=SPAC15E1.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-365.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
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 -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13860.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAB52424.1; -; Genomic_DNA.
DR EMBL; D89199; BAA13860.1; ALT_FRAME; mRNA.
DR PIR; T37720; T37720.
DR PIR; T42999; T42999.
DR RefSeq; NP_594306.1; NM_001019729.2.
DR AlphaFoldDB; Q9UTI6; -.
DR SMR; Q9UTI6; -.
DR BioGRID; 279224; 3.
DR STRING; 4896.SPAC15E1.05c.1; -.
DR MaxQB; Q9UTI6; -.
DR PaxDb; Q9UTI6; -.
DR EnsemblFungi; SPAC15E1.05c.1; SPAC15E1.05c.1:pep; SPAC15E1.05c.
DR PomBase; SPAC15E1.05c; -.
DR VEuPathDB; FungiDB:SPAC15E1.05c; -.
DR eggNOG; KOG2803; Eukaryota.
DR HOGENOM; CLU_031246_2_2_1; -.
DR InParanoid; Q9UTI6; -.
DR OMA; VLQCKYI; -.
DR PhylomeDB; Q9UTI6; -.
DR Reactome; R-SPO-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00742.
DR PRO; PR:Q9UTI6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004306; F:ethanolamine-phosphate cytidylyltransferase activity; ISO:PomBase.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IBA:GO_Central.
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; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 2: Evidence at transcript level;
KW Lipid biosynthesis; Lipid metabolism; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..365
FT /note="Probable ethanolamine-phosphate
FT cytidylyltransferase"
FT /id="PRO_0000208464"
FT REGION 344..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 63
FT /note="C -> G (in Ref. 2; BAA13860)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="I -> L (in Ref. 2; BAA13860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 41557 MW; ACDB6A974ABB4734 CRC64;
MASSSNIKHR LWLDGCMDFF HYGHSNAILQ AKQLGETLVI GIHSDEEITL NKGPPVMTLE
ERCLSANTCK WVDEVVPSAP YVFDLEWMRR YGCQYVVHGD DISTDANGDD CYRFAKAADQ
YLEVKRTEGV STTELLDRLL SSVPLEIYST PVSVLSSQID LLRRFATDSD GLTPFTDVFI
YNTEKPETLI SGTTLLRLNP EKNIIYIDGD WDLFTEKHIS ALELCTRMFP GIPIMAGIFA
DEKCFEKPML NLLERILNLL QCKYISSILV GPPPASLFAS SKYIKLCFDE QISKVYYPIF
STDVSIPALD ISLSNTPNNS FYKFDKLGSD LIKQRVMLRR QHYEERQRRK MGKNATEQTT
IKTYA
