DIPPS_THEKO
ID DIPPS_THEKO Reviewed; 432 AA.
AC Q5JDA9;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=TK2279;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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}.
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DR EMBL; AP006878; BAD86468.1; -; Genomic_DNA.
DR RefSeq; WP_011251229.1; NC_006624.1.
DR AlphaFoldDB; Q5JDA9; -.
DR SMR; Q5JDA9; -.
DR STRING; 69014.TK2279; -.
DR EnsemblBacteria; BAD86468; BAD86468; TK2279.
DR GeneID; 3234721; -.
DR KEGG; tko:TK2279; -.
DR PATRIC; fig|69014.16.peg.2234; -.
DR eggNOG; arCOG00673; Archaea.
DR HOGENOM; CLU_643435_0_0_2; -.
DR InParanoid; Q5JDA9; -.
DR OMA; MVSYSTE; -.
DR OrthoDB; 115624at2157; -.
DR PhylomeDB; Q5JDA9; -.
DR BRENDA; 2.7.7.74; 5246.
DR BRENDA; 2.7.8.34; 5246.
DR Proteomes; UP000000536; 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..432
FT /note="Bifunctional IPC transferase and DIPP synthase"
FT /id="PRO_0000424334"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 3..225
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000250"
FT REGION 226..426
FT /note="CDP-alcohol phosphatidyltransferases"
FT /evidence="ECO:0000250"
FT BINDING 9..11
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 432 AA; 48718 MW; 25D8A27E1F2DFC3C CRC64;
MVPERAVILA AGLGTRMGRK PKGLVRVAGR EILYRTIRLL QENGVKKFIV VTNERYAPLY
QEFIERHGFD AEIIINPEPE KGNGHSLHLA KEKVSGKFAL TMSDHVYSRD FIERAVRGRG
LIADREPRWV DIGEATKVQV KDEKVWKIGK RLKEWDAIDT GFFVLDDEIF KVTEILENEK
NGDYSLSEVM ERAKVSVTFV DGLGWTDVDT PEEIKRARRM LVRTAVKGTG DGFVSRHLNR
RISTRVSELL VEKVTPNQMT VVTFLLGIIS ALTTLVSLPL AGILYQLSSI LDGIDGELAR
AQLRTSKLGG YVDSILDRYV DGSFLALLAY ATINEPIWYF VALLALLGSV MVSYSTERFR
GAFCRDAYKE VPALRKLPGK RDERVFLTML FLLYQIAASI KALFLTLAVL TNFRVALTLY
FVVKKVSHPK TI
