DIPPS_AQUAE
ID DIPPS_AQUAE Reviewed; 428 AA.
AC O67379;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Name=spsI; OrderedLocusNames=aq_1367;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07344.1; -; Genomic_DNA.
DR PIR; H70418; H70418.
DR RefSeq; NP_213943.1; NC_000918.1.
DR RefSeq; WP_010880881.1; NC_000918.1.
DR AlphaFoldDB; O67379; -.
DR SMR; O67379; -.
DR STRING; 224324.aq_1367; -.
DR EnsemblBacteria; AAC07344; AAC07344; aq_1367.
DR KEGG; aae:aq_1367; -.
DR PATRIC; fig|224324.8.peg.1070; -.
DR eggNOG; COG0558; Bacteria.
DR eggNOG; COG1213; Bacteria.
DR HOGENOM; CLU_643435_0_0_0; -.
DR InParanoid; O67379; -.
DR OMA; MVSYSTE; -.
DR OrthoDB; 1408846at2; -.
DR BRENDA; 2.7.7.74; 396.
DR BRENDA; 2.7.8.34; 396.
DR Proteomes; UP000000798; 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; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR Pfam; PF00483; NTP_transferase; 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..428
FT /note="Bifunctional IPC transferase and DIPP synthase"
FT /id="PRO_0000424333"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 2..227
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000250"
FT REGION 228..425
FT /note="CDP-alcohol phosphatidyltransferases"
FT /evidence="ECO:0000250"
FT BINDING 8..10
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 428 AA; 48501 MW; CC93F489A3B1F7A3 CRC64;
MVETAVILAG GEGNRLKPLT EEVPKALLKV AGRELLYRTI KQLQDVGVKN FVIVVNKKFE
GKVKAFLKEH NFEAEVIPNE HPEKENGYSL YLAKGRIKGE FAVVMSDHIY EKAFLEKAVE
GKGLIVDRLG LYINKNEATK VKCEEGRIKY IGKNLEKYDG FDTGFFVLDE SIFEVAEEAL
KEQKKLTMSE LAKRAQIPCT EVSGYFWMDV DTPEDVEKAK KYLVKTAIKG VGDGFISRNL
NRKVSTRISP YLVDKFTPNQ LTVLTFLLGM FSALVAYFSP ALGGILLQIN SMLDGLDGEV
ARAQMRTTKF GAWLDSVLDR YVDFAFLSAL AMHLKPSWDF MPWVFAALFG SVMVSYSTER
YKGAYCEDAY AVIKELRYLL GKRDERIFMI MIFTILGWIK ALFVVLAIIT NLRVILTIYL
VWKKKGNV
