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Protein

Bifunctional IPC transferase and DIPP synthase

Gene

AF_0263

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate. The cytidylyltransferase is absolutely specific for CTP and L-myo-inositol-1-P. The DIPP synthase uses only L-myoinositol-1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-L-myo-inositol and CDP-D-myoinositol, are recognized as alcohol donors.3 Publications

Catalytic activityi

CTP + 1L-myo-inositol 1-phosphate = diphosphate + CDP-1L-myo-inositol.1 Publication
CDP-1L-myo-inositol + 1L-myo-inositol 1-phosphate = CMP + bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate.1 Publication

Cofactori

Mg2+By similarity

Kineticsi

  1. KM=0.58 mM for CTP (at pH 7 and 90 degrees Celsius)1 Publication
  2. KM=0.87 mM for Inositol-1-phosphate (at pH 7 and 90 degrees Celsius)1 Publication
  1. Vmax=62.9 µmol/min/mg enzyme (at pH 7 and 90 degrees Celsius)1 Publication

pH dependencei

Optimum pH is between 6.5 and 7.5.1 Publication

Temperature dependencei

Optimum temperature is between 90 and 95 degrees Celsius. The activity is undetectable at temperatures below 60 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911CTPBy similarity
Binding sitei144 – 1441CTPBy similarity
Metal bindingi180 – 1801MagnesiumBy similarity
Binding sitei180 – 1801CTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi78 – 803CTPBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • nucleotidyltransferase activity Source: UniProtKB
  • phosphotransferase activity, for other substituted phosphate groups Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-271-MONOMER.
MetaCyc:MONOMER-16017.
BRENDAi2.7.7.74. 414.
2.7.8.34. 414.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional IPC transferase and DIPP synthase
Including the following 2 domains:
1L-myo-inositol-1-phosphate cytidylyltransferase (EC:2.7.7.74)
Short name:
IPCT
CDP-L-myo-inositol myo-inositolphosphotransferase (EC:2.7.8.34)
Short name:
DIPP synthase
Alternative name(s):
Di-myo-inositol-1,3'-phosphate-1'-phosphate synthase
Gene namesi
Ordered Locus Names:AF_0263
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei329 – 34921HelicalSequence analysisAdd
BLAST
Transmembranei389 – 40921HelicalSequence analysisAdd
BLAST
Transmembranei447 – 46721HelicalSequence analysisAdd
BLAST
Transmembranei468 – 48821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490Bifunctional IPC transferase and DIPP synthasePRO_0000424330Add
BLAST

Interactioni

Subunit structurei

Forms a mixture of monomers and dimers in solution, with prevalence of the monomeric form.1 Publication

Protein-protein interaction databases

STRINGi224325.AF0263.

Structurei

Secondary structure

1
490
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi73 – 797Combined sources
Helixi91 – 933Combined sources
Beta strandi95 – 1006Combined sources
Helixi101 – 1099Combined sources
Helixi110 – 1123Combined sources
Beta strandi113 – 1219Combined sources
Helixi124 – 1318Combined sources
Helixi132 – 1343Combined sources
Beta strandi138 – 1425Combined sources
Helixi146 – 1483Combined sources
Helixi150 – 1556Combined sources
Helixi156 – 1605Combined sources
Beta strandi163 – 1697Combined sources
Beta strandi172 – 1743Combined sources
Helixi176 – 1827Combined sources
Beta strandi187 – 1937Combined sources
Beta strandi195 – 1973Combined sources
Turni199 – 2013Combined sources
Beta strandi204 – 2085Combined sources
Beta strandi211 – 2166Combined sources
Beta strandi223 – 23210Combined sources
Helixi236 – 2405Combined sources
Helixi241 – 2433Combined sources
Helixi251 – 2588Combined sources
Beta strandi261 – 2644Combined sources
Beta strandi270 – 2745Combined sources
Helixi276 – 28813Combined sources
Helixi298 – 3025Combined sources
Helixi304 – 31512Combined sources
Turni316 – 3183Combined sources
Helixi321 – 33717Combined sources
Helixi338 – 3403Combined sources
Helixi343 – 35614Combined sources
Helixi359 – 3668Combined sources
Helixi372 – 39625Combined sources
Helixi398 – 4003Combined sources
Helixi401 – 42525Combined sources
Helixi443 – 45715Combined sources
Helixi462 – 48726Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XMEX-ray1.89A/B/C/D/E/F/G/H/I/J/K/L55-286[»]
2XMHX-ray2.40A/B/C/D/E/F55-286[»]
4MNDX-ray2.66A55-490[»]
ProteinModelPortaliO29976.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO29976.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni72 – 290219MobA-like NTP transferaseAdd
BLAST
Regioni291 – 490200CDP-alcohol phosphatidyltransferasesAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the MobA family.Curated
In the C-terminal section; belongs to the CDP-alcohol phosphatidyltransferase class-I family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG00670. Archaea.
arCOG00673. Archaea.
COG0558. LUCA.
COG1213. LUCA.
KOiK07281.
K07291.
OMAiMVSYSTE.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR000462. CDP-OH_P_trans.
IPR025877. MobA-like_NTP_Trfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01066. CDP-OH_P_transf. 1 hit.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O29976-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILPCESFNG VPSGCLIIEM NWYSVLKAST AIFFPEKYSS STSSLSKRSP
60 70 80 90 100
ISAPMINVDG EYLKIFAGRI KLMKAVILAA GLGTRLGGVP KPLVRVGGCE
110 120 130 140 150
IILRTMKLLS PHVSEFIIVA SRYADDIDAF LKDKGFNYKI VRHDRPEKGN
160 170 180 190 200
GYSLLVAKNH VEDRFILTMG DHVYSQQFIE KAVRGEGVIA DREPRFVDIG
210 220 230 240 250
EATKIRVEDG RVAKIGKDLR EFDCVDTGFF VLDDSIFEHA EKLRDREEIP
260 270 280 290 300
LSEIVKLARL PVTYVDGELW MDVDTKEDVR RANRALVSAA VKGSGDGFIS
310 320 330 340 350
RKINRKISTR ISAAIVNKVN PNQMTLISFL VGAFSALASF FSIPLAGLLY
360 370 380 390 400
QFSSILDGCD GEIARASLKM SKKGGYVDSI LDRFVDFLFL AIIALLYPKT
410 420 430 440 450
ATVAMFAIFG SVMVSYTSEK YKAEFGESIF GKFRVLNYIP GKRDERIFLI
460 470 480 490
MIFCLLSAIS LQWIFWMFLF VAAISLTRVV VTLLAVLVSK
Length:490
Mass (Da):54,560
Last modified:January 1, 1998 - v1
Checksum:i7E10FD48866BA66D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90972.1.
PIRiG69282.

Genome annotation databases

EnsemblBacteriaiAAB90972; AAB90972; AF_0263.
KEGGiafu:AF_0263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90972.1.
PIRiG69282.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XMEX-ray1.89A/B/C/D/E/F/G/H/I/J/K/L55-286[»]
2XMHX-ray2.40A/B/C/D/E/F55-286[»]
4MNDX-ray2.66A55-490[»]
ProteinModelPortaliO29976.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF0263.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB90972; AAB90972; AF_0263.
KEGGiafu:AF_0263.

Phylogenomic databases

eggNOGiarCOG00670. Archaea.
arCOG00673. Archaea.
COG0558. LUCA.
COG1213. LUCA.
KOiK07281.
K07291.
OMAiMVSYSTE.

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-271-MONOMER.
MetaCyc:MONOMER-16017.
BRENDAi2.7.7.74. 414.
2.7.8.34. 414.

Miscellaneous databases

EvolutionaryTraceiO29976.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR000462. CDP-OH_P_trans.
IPR025877. MobA-like_NTP_Trfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01066. CDP-OH_P_transf. 1 hit.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDIPPS_ARCFU
AccessioniPrimary (citable) accession number: O29976
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2013
Last sequence update: January 1, 1998
Last modified: November 11, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.