DIPPS_PYRFU
ID DIPPS_PYRFU Reviewed; 430 AA.
AC Q8U1Z6;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Bifunctional IPC transferase and DIPP synthase;
DE Includes:
DE RecName: Full=1L-myo-inositol-1-phosphate cytidylyltransferase;
DE Short=IPCT;
DE EC=2.7.7.74;
DE Includes:
DE RecName: Full=CDP-L-myo-inositol myo-inositolphosphotransferase;
DE Short=DIPP synthase;
DE EC=2.7.8.34;
DE AltName: Full=Di-myo-inositol-1,3'-phosphate-1'-phosphate synthase;
GN OrderedLocusNames=PF1058;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17526717; DOI=10.1128/jb.00465-07;
RA Rodrigues M.V., Borges N., Henriques M., Lamosa P., Ventura R.,
RA Fernandes C., Empadinhas N., Maycock C., da Costa M.S., Santos H.;
RT "Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-
RT inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-
RT inositol-phosphate synthesis in several (hyper)thermophiles.";
RL J. Bacteriol. 189:5405-5412(2007).
CC -!- FUNCTION: Involved in biosynthesis of di-myo-inositol phosphate (DIP),
CC a widespread organic solute in microorganisms adapted to hot
CC environments. Catalyzes the condensation of CTP and L-myo-inositol-1-
CC phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-
CC myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol
CC and L-myo-inositol-1-phosphate. {ECO:0000269|PubMed:17526717}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3-phosphate + CTP + H(+) = CDP-1L-myo-inositol
CC + diphosphate; Xref=Rhea:RHEA:30647, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58401,
CC ChEBI:CHEBI:62573; EC=2.7.7.74;
CC Evidence={ECO:0000269|PubMed:17526717};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3-phosphate + CDP-1L-myo-inositol = bis(1L-
CC myo-inositol) 3,1'-phosphate 1-phosphate + CMP + H(+);
CC Xref=Rhea:RHEA:31327, ChEBI:CHEBI:15378, ChEBI:CHEBI:58401,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:62573, ChEBI:CHEBI:62576; EC=2.7.8.34;
CC Evidence={ECO:0000269|PubMed:17526717};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MobA family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the CDP-alcohol
CC phosphatidyltransferase class-I family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE009950; AAL81182.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8U1Z6; -.
DR SMR; Q8U1Z6; -.
DR STRING; 186497.PF1058; -.
DR EnsemblBacteria; AAL81182; AAL81182; PF1058.
DR KEGG; pfu:PF1058; -.
DR PATRIC; fig|186497.12.peg.1119; -.
DR eggNOG; arCOG00673; Archaea.
DR HOGENOM; CLU_643435_0_0_2; -.
DR OMA; MVSYSTE; -.
DR PhylomeDB; Q8U1Z6; -.
DR BRENDA; 2.7.7.74; 5243.
DR BRENDA; 2.7.8.34; 5243.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.120.1760; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW Magnesium; Membrane; Metal-binding; Multifunctional enzyme;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..430
FT /note="Bifunctional IPC transferase and DIPP synthase"
FT /id="PRO_0000424332"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 8..230
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000250"
FT REGION 231..428
FT /note="CDP-alcohol phosphatidyltransferases"
FT /evidence="ECO:0000250"
FT BINDING 14..16
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 430 AA; 48738 MW; FA48115D1633D759 CRC64;
MNILGGEEVK GVILAAGYGS RMGEKPKGLL KIAGREILYR TIKNLEKNGI KEFIIVTNER
YLQKFEEFVK ENNLQNVKLA VNRFPEKGNG YSLYVAKDFV KGKFVLVMSD HIYEEKFYEL
ALRGEGLIVD RNPKFVDIDE ATKVKIENDR VVDIGKEIPS WDGVDTGFFI LDDSIFSVIE
DILKEKEVVE LKDVVKRARL KVSYVDGLYW MDVDTPGDLK KARKLIVYSS VKGVGDGFIS
RYINRKISTR ISALLVDHIT PNKLTIVTFL FGIFSGLMNL ISVPLAAILY QISSIFDGVD
GEIARARMQT SKFGGFFDSI LDRYVDFTYL LTLAYVTIRE PIWWVIAGIA IFSSAMVSYS
TERFRGAYCA DAYKVVPALR KIPGKRDERI FVTMIFALLG LIKPLFALLA AWSTLRVIIT
IYLVWRDVNG
