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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)DescriptionActionsGraphical viewLength
Binding sitei91CTPBy similarity1
Binding sitei144CTPBy similarity1
Metal bindingi180MagnesiumBy similarity1
Binding sitei180CTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi78 – 80CTPBy similarity3

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

BioCyciMetaCyc: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)DescriptionActionsGraphical viewLength
Transmembranei329 – 349HelicalSequence analysisAdd BLAST21
Transmembranei389 – 409HelicalSequence analysisAdd BLAST21
Transmembranei447 – 467HelicalSequence analysisAdd BLAST21
Transmembranei468 – 488HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004243301 – 490Bifunctional IPC transferase and DIPP synthaseAdd BLAST490

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

1490
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi73 – 79Combined sources7
Helixi91 – 93Combined sources3
Beta strandi95 – 100Combined sources6
Helixi101 – 109Combined sources9
Helixi110 – 112Combined sources3
Beta strandi113 – 121Combined sources9
Helixi124 – 131Combined sources8
Helixi132 – 134Combined sources3
Beta strandi138 – 142Combined sources5
Helixi146 – 148Combined sources3
Helixi150 – 155Combined sources6
Helixi156 – 160Combined sources5
Beta strandi163 – 169Combined sources7
Beta strandi172 – 174Combined sources3
Helixi176 – 182Combined sources7
Beta strandi187 – 193Combined sources7
Beta strandi195 – 197Combined sources3
Turni199 – 201Combined sources3
Beta strandi204 – 208Combined sources5
Beta strandi211 – 216Combined sources6
Beta strandi223 – 232Combined sources10
Helixi236 – 240Combined sources5
Helixi241 – 243Combined sources3
Helixi251 – 258Combined sources8
Beta strandi261 – 264Combined sources4
Beta strandi270 – 274Combined sources5
Helixi276 – 288Combined sources13
Helixi298 – 302Combined sources5
Helixi304 – 315Combined sources12
Turni316 – 318Combined sources3
Helixi321 – 337Combined sources17
Helixi338 – 340Combined sources3
Helixi343 – 356Combined sources14
Helixi359 – 366Combined sources8
Helixi372 – 396Combined sources25
Helixi398 – 400Combined sources3
Helixi401 – 425Combined sources25
Helixi443 – 457Combined sources15
Helixi462 – 487Combined sources26

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiO29976.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO29976.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni72 – 290MobA-like NTP transferaseAdd BLAST219
Regioni291 – 490CDP-alcohol phosphatidyltransferasesAdd BLAST200

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
PDB 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.
SMRiO29976.
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

BioCyciMetaCyc: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 2, 2016
This is version 95 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.