ID DIPPS_ARCFU Reviewed; 490 AA.
AC O29976;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 121.
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=AF_0263;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION.
RX PubMed=17028285; DOI=10.1128/jb.01129-06;
RA Borges N., Goncalves L.G., Rodrigues M.V., Siopa F., Ventura R.,
RA Maycock C., Lamosa P., Santos H.;
RT "Biosynthetic pathways of inositol and glycerol phosphodiesters used by the
RT hyperthermophile Archaeoglobus fulgidus in stress adaptation.";
RL J. Bacteriol. 188:8128-8135(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 55-286, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=21378188; DOI=10.1128/jb.01543-10;
RA Brito J.A., Borges N., Vonrhein C., Santos H., Archer M.;
RT "Crystal structure of Archaeoglobus fulgidus CTP:inositol-1-phosphate
RT cytidylyltransferase, a key enzyme for di-myo-inositol-phosphate synthesis
RT in (hyper)thermophiles.";
RL J. Bacteriol. 193:2177-2185(2011).
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. The cytidylyltransferase is absolutely
CC specific for CTP and L-myo-inositol-1-P. The DIPP synthase uses only L-
CC myoinositol-1-phosphate as an alcohol acceptor, but CDP-glycerol, as
CC well as CDP-L-myo-inositol and CDP-D-myoinositol, are recognized as
CC alcohol donors. {ECO:0000269|PubMed:17028285,
CC ECO:0000269|PubMed:17526717, ECO:0000269|PubMed:21378188}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.58 mM for CTP (at pH 7 and 90 degrees Celsius)
CC {ECO:0000269|PubMed:21378188};
CC KM=0.87 mM for Inositol-1-phosphate (at pH 7 and 90 degrees Celsius)
CC {ECO:0000269|PubMed:21378188};
CC Vmax=62.9 umol/min/mg enzyme (at pH 7 and 90 degrees Celsius)
CC {ECO:0000269|PubMed:21378188};
CC pH dependence:
CC Optimum pH is between 6.5 and 7.5. {ECO:0000269|PubMed:21378188};
CC Temperature dependence:
CC Optimum temperature is between 90 and 95 degrees Celsius. The
CC activity is undetectable at temperatures below 60 degrees Celsius.
CC {ECO:0000269|PubMed:21378188};
CC -!- SUBUNIT: Forms a mixture of monomers and dimers in solution, with
CC prevalence of the monomeric form. {ECO:0000269|PubMed:21378188}.
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; AE000782; AAB90972.1; -; Genomic_DNA.
DR PIR; G69282; G69282.
DR PDB; 2XME; X-ray; 1.89 A; A/B/C/D/E/F/G/H/I/J/K/L=55-286.
DR PDB; 2XMH; X-ray; 2.40 A; A/B/C/D/E/F=55-286.
DR PDB; 4MND; X-ray; 2.66 A; A=55-490.
DR PDBsum; 2XME; -.
DR PDBsum; 2XMH; -.
DR PDBsum; 4MND; -.
DR AlphaFoldDB; O29976; -.
DR SMR; O29976; -.
DR STRING; 224325.AF_0263; -.
DR PaxDb; 224325-AF_0263; -.
DR EnsemblBacteria; AAB90972; AAB90972; AF_0263.
DR KEGG; afu:AF_0263; -.
DR eggNOG; arCOG00673; Archaea.
DR HOGENOM; CLU_643435_0_0_2; -.
DR PhylomeDB; O29976; -.
DR BioCyc; MetaCyc:MONOMER-16017; -.
DR BRENDA; 2.7.7.74; 414.
DR BRENDA; 2.7.8.34; 414.
DR EvolutionaryTrace; O29976; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; NF041135; IPPtranDIPPsyn_Thcocales; 1.
DR PANTHER; PTHR19136:SF84; BIFUNCTIONAL IPC TRANSFERASE AND DIPP SYNTHASE; 1.
DR PANTHER; PTHR19136; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Membrane; Metal-binding; Multifunctional enzyme;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..490
FT /note="Bifunctional IPC transferase and DIPP synthase"
FT /id="PRO_0000424330"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 72..290
FT /note="MobA-like NTP transferase"
FT REGION 291..490
FT /note="CDP-alcohol phosphatidyltransferases"
FT BINDING 78..80
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2XME"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:2XMH"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2XME"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4MND"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:2XME"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:2XME"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:2XME"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:2XME"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2XME"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:2XME"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:2XME"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:2XME"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:2XME"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:2XME"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:2XME"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:4MND"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:4MND"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:4MND"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:4MND"
FT HELIX 321..337
FT /evidence="ECO:0007829|PDB:4MND"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:4MND"
FT HELIX 343..356
FT /evidence="ECO:0007829|PDB:4MND"
FT HELIX 359..366
FT /evidence="ECO:0007829|PDB:4MND"
FT HELIX 372..396
FT /evidence="ECO:0007829|PDB:4MND"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:4MND"
FT HELIX 401..425
FT /evidence="ECO:0007829|PDB:4MND"
FT HELIX 443..457
FT /evidence="ECO:0007829|PDB:4MND"
FT HELIX 462..487
FT /evidence="ECO:0007829|PDB:4MND"
SQ SEQUENCE 490 AA; 54560 MW; 7E10FD48866BA66D CRC64;
MILPCESFNG VPSGCLIIEM NWYSVLKAST AIFFPEKYSS STSSLSKRSP ISAPMINVDG
EYLKIFAGRI KLMKAVILAA GLGTRLGGVP KPLVRVGGCE IILRTMKLLS PHVSEFIIVA
SRYADDIDAF LKDKGFNYKI VRHDRPEKGN GYSLLVAKNH VEDRFILTMG DHVYSQQFIE
KAVRGEGVIA DREPRFVDIG EATKIRVEDG RVAKIGKDLR EFDCVDTGFF VLDDSIFEHA
EKLRDREEIP LSEIVKLARL PVTYVDGELW MDVDTKEDVR RANRALVSAA VKGSGDGFIS
RKINRKISTR ISAAIVNKVN PNQMTLISFL VGAFSALASF FSIPLAGLLY QFSSILDGCD
GEIARASLKM SKKGGYVDSI LDRFVDFLFL AIIALLYPKT ATVAMFAIFG SVMVSYTSEK
YKAEFGESIF GKFRVLNYIP GKRDERIFLI MIFCLLSAIS LQWIFWMFLF VAAISLTRVV
VTLLAVLVSK
//
