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Protein

Fructose-1,6-bisphosphatase/inositol-1-monophosphatase

Gene

suhB

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

Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate and fructose-6-phosphate. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.3 Publications

Catalytic activityi

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.2 Publications
Myo-inositol phosphate + H2O = myo-inositol + phosphate.3 Publications

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Magnesium. Can also use manganese.1 Publication

Enzyme regulationi

Both FBPase and IMPase activities are inhibited by Ca2+. In contrast to mammalian I-1-P phosphatases, is only very weakly inhibited by Li+ (with an IC50 of about 290 mM).1 Publication

Kineticsi

kcat is 2.5 sec(-1) for IMPase activity (at 85 degrees Celsius) and 2.7 sec(-1) for FBPase activity (at 85 degrees Celsius).1 Publication

Manual assertion based on experiment ini

  1. KM=0.11 mM for inositol-1-phosphate (at 85 degrees Celsius)2 Publications
  2. KM=0.08 mM for D-fructose 1,6-bisphosphate (at 85 degrees Celsius)2 Publications
  1. Vmax=3.27 µmol/min/mg enzyme with L-inositol-1-phosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mg2+)2 Publications
  2. Vmax=2.20 µmol/min/mg enzyme with L-inositol-1-phosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mn2+)2 Publications
  3. Vmax=1.52 µmol/min/mg enzyme with D-fructose 1,6-bisphosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mg2+)2 Publications
  4. Vmax=1.92 µmol/min/mg enzyme with D-fructose 1,6-bisphosphate as substrate (at 80 degrees Celsius, pH 8, in the presence of Mn2+)2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi38Magnesium 31
Metal bindingi40Magnesium 31
Metal bindingi67Magnesium 11
Metal bindingi67Magnesium 31
Metal bindingi82Magnesium 11
Metal bindingi82Magnesium 21
Metal bindingi84Magnesium 1; via carbonyl oxygen1
Metal bindingi85Magnesium 21
Binding sitei167Substrate1
Binding sitei172Substrate; via amide nitrogen1
Binding sitei191Substrate1
Metal bindingi200Magnesium 21

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.11. 414.
3.1.3.25. 414.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase/inositol-1-monophosphatase (EC:3.1.3.112 Publications, EC:3.1.3.253 Publications)
Short name:
FBPase/IMPase
Alternative name(s):
Inositol-1-phosphatase
Short name:
I-1-Pase
Gene namesi
Name:suhB
Ordered Locus Names:AF_2372
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001425791 – 252Fructose-1,6-bisphosphatase/inositol-1-monophosphataseAdd BLAST252

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224325.AF2372.

Structurei

Secondary structure

1252
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 22Combined sources20
Helixi26 – 29Combined sources4
Beta strandi32 – 35Combined sources4
Beta strandi37 – 43Combined sources7
Helixi44 – 57Combined sources14
Beta strandi60 – 66Combined sources7
Turni67 – 69Combined sources3
Beta strandi70 – 72Combined sources3
Beta strandi76 – 85Combined sources10
Helixi87 – 91Combined sources5
Beta strandi98 – 108Combined sources11
Helixi109 – 111Combined sources3
Beta strandi112 – 119Combined sources8
Turni120 – 122Combined sources3
Beta strandi125 – 129Combined sources5
Beta strandi132 – 135Combined sources4
Beta strandi138 – 140Combined sources3
Beta strandi147 – 155Combined sources9
Beta strandi164 – 168Combined sources5
Helixi172 – 180Combined sources9
Beta strandi183 – 189Combined sources7
Helixi198 – 210Combined sources13
Beta strandi214 – 216Combined sources3
Beta strandi227 – 230Combined sources4
Beta strandi236 – 239Combined sources4
Turni241 – 243Combined sources3
Helixi244 – 251Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LBVX-ray1.80A/B1-252[»]
1LBWX-ray2.00A/B1-252[»]
1LBXX-ray2.40A/B1-252[»]
1LBYX-ray2.25A/B1-252[»]
1LBZX-ray2.20A/B1-252[»]
ProteinModelPortaliO30298.
SMRiO30298.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO30298.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni85 – 87Substrate binding3

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiarCOG01349. Archaea.
COG0483. LUCA.
KOiK01092.
OMAiNNEYLAN.

Family and domain databases

InterProiIPR000760. Inositol_monophosphatase-like.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O30298-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDERDALRIS REIAGEVRKA IASMPLRERV KDVGMGKDGT PTKAADRVAE
60 70 80 90 100
DAALEILRKE RVTVVTEESG VLGEGDVFVA LDPLDGTFNA TRGIPVYSVS
110 120 130 140 150
LCFSYSDKLK DAFFGYVYNL ATGDEYYADS SGAYRNGERI EVSDAEELYC
160 170 180 190 200
NAIIYYPDRK FPFKRMRIFG SAATELCFFA DGSFDCFLDI RPGKMLRIYD
210 220 230 240 250
AAAGVFIAEK AGGKVTELDG ESLGNKKFDM QERLNIVAAN EKLHPKLLEL

IK
Length:252
Mass (Da):27,967
Last modified:January 1, 1998 - v1
Checksum:iEF48983721AEA687
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB91288.1.
PIRiD69546.
RefSeqiWP_010879859.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB91288; AAB91288; AF_2372.
GeneIDi24796117.
KEGGiafu:AF_2372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB91288.1.
PIRiD69546.
RefSeqiWP_010879859.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LBVX-ray1.80A/B1-252[»]
1LBWX-ray2.00A/B1-252[»]
1LBXX-ray2.40A/B1-252[»]
1LBYX-ray2.25A/B1-252[»]
1LBZX-ray2.20A/B1-252[»]
ProteinModelPortaliO30298.
SMRiO30298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF2372.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB91288; AAB91288; AF_2372.
GeneIDi24796117.
KEGGiafu:AF_2372.

Phylogenomic databases

eggNOGiarCOG01349. Archaea.
COG0483. LUCA.
KOiK01092.
OMAiNNEYLAN.

Enzyme and pathway databases

BRENDAi3.1.3.11. 414.
3.1.3.25. 414.

Miscellaneous databases

EvolutionaryTraceiO30298.

Family and domain databases

InterProiIPR000760. Inositol_monophosphatase-like.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBSUHB_ARCFU
AccessioniPrimary (citable) accession number: O30298
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 121 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, 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.