DIPPS_RUBXD
ID DIPPS_RUBXD Reviewed; 436 AA.
AC Q1AWQ0; A7KPU8;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Rxyl_1212;
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; EF523341; ABS30690.1; -; Genomic_DNA.
DR EMBL; CP000386; ABG04178.1; -; Genomic_DNA.
DR RefSeq; WP_011564196.1; NC_008148.1.
DR AlphaFoldDB; Q1AWQ0; -.
DR SMR; Q1AWQ0; -.
DR STRING; 266117.Rxyl_1212; -.
DR EnsemblBacteria; ABG04178; ABG04178; Rxyl_1212.
DR KEGG; rxy:Rxyl_1212; -.
DR eggNOG; COG0558; Bacteria.
DR eggNOG; COG1213; Bacteria.
DR HOGENOM; CLU_643435_0_0_11; -.
DR OrthoDB; 1408846at2; -.
DR PhylomeDB; Q1AWQ0; -.
DR BRENDA; 2.7.7.74; 10017.
DR Proteomes; UP000006637; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; 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 Membrane; Multifunctional enzyme; Nucleotidyltransferase;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..436
FT /note="Bifunctional IPC transferase and DIPP synthase"
FT /id="PRO_0000424331"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 11..241
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000250"
FT REGION 242..435
FT /note="CDP-alcohol phosphatidyltransferases"
FT /evidence="ECO:0000250"
FT BINDING 17..19
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT CONFLICT 3..11
FT /note="DERTTGREG -> ETERRGDS (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="R -> C (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="E -> D (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="V -> A (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="E -> D (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="H -> Y (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="A -> E (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="I -> V (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="E -> D (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="R -> G (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..155
FT /note="LEG -> IES (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="E -> D (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="R -> E (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="P -> L (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..192
FT /note="SGG -> AGQ (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="Q -> R (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="R -> H (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="V -> I (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="L -> F (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="T -> A (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="L -> A (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="A -> V (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="I -> V (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="L -> V (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="L -> R (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="R -> G (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 405..410
FT /note="LLGAPG -> MLRAPV (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="A -> I (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
FT CONFLICT 433..436
FT /note="RGRS -> KERT (in Ref. 1; ABS30690)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 46105 MW; 0CB20E027B8C856A CRC64;
MPDERTTGRE GVGAAVLAAG FGERLRECGR PKPLARVAGL TLLERTVRTL RAGGLEGEIV
VVVGHRGEEV AGHCKARGLP VRVVENPDYP RGNGTSVLAA MRFLPERFVV AMVDHIHTPE
SVRRLLRCEG DFVAAVDTRP VYADPGEATR VRLEGGRVVE FGKNLPRYDG LDAGLFLCSR
PALERLREAS GGERLSWNDL KRAWLASGGE VVACDLAGAP WTDVDTPQDL RLSEEMVLGW
AASGNDGPVS RHINRRISRR ITRRLLDTPL SPDQVSLLSF ALAALGAGLL AAGRLRLGGA
LVQLASIVDG CDGELARARL ESSPRGAVFD ATLDRWADAL IISGLALGAG TRLAAAAGYP
ALAGALLVSY TRARWEAALG RMPSRFTGLG ATRDVRLAVL ALGGLLGAPG AALLATGALG
NAEALRRLLA LKRGRS
