ID C1HC09_PARBA Unreviewed; 457 AA.
AC C1HC09;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269};
DE EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269};
GN ORFNames=PAAG_08300 {ECO:0000313|EMBL:EEH38573.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH38573.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH38573.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001698,
CC ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005119, ECO:0000256|PIRNR:PIRNR018269,
CC ECO:0000256|RuleBase:RU003938}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000256|ARBA:ARBA00010185,
CC ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}.
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DR EMBL; KN294022; EEH38573.2; -; Genomic_DNA.
DR RefSeq; XP_015701136.1; XM_015846472.1.
DR AlphaFoldDB; C1HC09; -.
DR STRING; 502779.C1HC09; -.
DR GeneID; 9093061; -.
DR KEGG; pbl:PAAG_08300; -.
DR VEuPathDB; FungiDB:PAAG_08300; -.
DR eggNOG; KOG1440; Eukaryota.
DR HOGENOM; CLU_023471_1_1_1; -.
DR OMA; FFAYMYF; -.
DR OrthoDB; 5481516at2759; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniRule.
DR InterPro; IPR000374; PC_trans.
DR InterPro; IPR016720; PC_Trfase_euk.
DR PANTHER; PTHR13773; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR13773:SF8; PHOSPHATIDATE CYTIDYLYLTRANSFERASE, PHOTORECEPTOR-SPECIFIC; 1.
DR Pfam; PF01148; CTP_transf_1; 1.
DR PIRSF; PIRSF018269; PC_trans_euk; 1.
DR PROSITE; PS01315; CDS; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR018269};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR018269};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR018269}.
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 93..114
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 126..147
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 167..184
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 196..214
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 220..246
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 258..276
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 51960 MW; E09DD6CDB99AC586 CRC64;
MGRLRRNVRF QHRPASTDPR QSSDLSDISE PSSPSNNGVS GSKAVEVVPE EKSDAAPPSD
YEKKKQTFIT RTIWTFVMIA GFFIAIFSGH IYIIAIITVV QIISFKEVIA IANVPSKAKN
LKFTKALNWY FLATTMYFLY GESVIYYFKH ILLVDRVLLP LATHHRFISF MLYVMGFVFF
VGSLQKGHYR FQFTQFAWTH MALYLIVVQA HFIMNNIFEG MIWFFLPVSL VITNDIFAYI
CGITFGRTQL IKLSPKKTVE GFVGAWICTI LFGYGMTNIL MKYKYFICPV NDLGSNVLTG
LECTPNPVFT PHPYQILSWA PWTHAPPRTV YFAPMQIHIF VFATFASLIA PFGGFFASGL
KRTFKVKDFG ESIPGHGGIT DRMDCQFIMG FFAYMYYHSF IAVYKASVGN VIEAAITGLT
VDQQLEVIRG LTKYLYNQGE VSETMLECLS PDFRVSR
//
