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Protein

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

Gene

suhB

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
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, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, NAD+ or 5'-AMP. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.2 Publications

Catalytic activityi

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

Cofactori

Mg2+1 Publication

Enzyme regulationi

IMPase activity is inhibited by Ca2+ and Zn2+. In contrast to mammalian I-1-P phosphatases, is not inhibited by Li+ up to 100 mM.1 Publication

Kineticsi

kcat is 4.2 sec(-1) for IMPase activity (at 85 degrees Celsius) and 7.0 sec(-1) for FBPase activity (at 85 degrees Celsius).

  1. KM=0.091 mM for inositol-1-phosphate (at 85 degrees Celsius)2 Publications
  2. KM=0.038 mM for D-fructose 1,6-bisphosphate (at 85 degrees Celsius)2 Publications
  1. Vmax=9.3 µmol/min/mg enzyme for IMPase activity (at 85 degrees Celsius)2 Publications

Temperature dependencei

Is thermostable. After incubation at 85 degrees Celsius for 30 minutes, more than 95% of I-1-Pase activity remains.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi65 – 651Magnesium 12 Publications
Metal bindingi81 – 811Magnesium 12 Publications
Metal bindingi81 – 811Magnesium 22 Publications
Metal bindingi83 – 831Magnesium 1; via carbonyl oxygen2 Publications
Metal bindingi84 – 841Magnesium 22 Publications
Binding sitei170 – 1701Substrate1 Publication
Binding sitei175 – 1751Substrate; via amide nitrogen1 Publication
Binding sitei194 – 1941Substrate1 Publication
Metal bindingi201 – 2011Magnesium 22 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-5062.
BRENDAi3.1.3.25. 3260.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase/inositol-1-monophosphatase (EC:3.1.3.111 Publication, EC:3.1.3.252 Publications)
Short name:
FBPase/IMPase
Alternative name(s):
Inositol-1-phosphatase
Short name:
I-1-Pase
Gene namesi
Name:suhB
Ordered Locus Names:MJ0109
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 252252Fructose-1,6-bisphosphatase/inositol-1-monophosphatasePRO_0000142580Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi243232.MJ_0109.

Structurei

Secondary structure

1
252
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1816Combined sources
Helixi19 – 213Combined sources
Turni25 – 273Combined sources
Beta strandi30 – 345Combined sources
Turni35 – 373Combined sources
Beta strandi38 – 414Combined sources
Helixi42 – 5514Combined sources
Helixi56 – 583Combined sources
Beta strandi60 – 645Combined sources
Helixi65 – 673Combined sources
Beta strandi68 – 703Combined sources
Beta strandi75 – 8410Combined sources
Helixi86 – 905Combined sources
Beta strandi97 – 11519Combined sources
Helixi116 – 1183Combined sources
Beta strandi120 – 1256Combined sources
Turni126 – 1283Combined sources
Beta strandi129 – 1324Combined sources
Helixi144 – 1463Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi155 – 1573Combined sources
Helixi159 – 1657Combined sources
Beta strandi167 – 1693Combined sources
Helixi175 – 1839Combined sources
Beta strandi188 – 1925Combined sources
Helixi199 – 21012Combined sources
Turni211 – 2133Combined sources
Beta strandi215 – 2173Combined sources
Beta strandi219 – 2235Combined sources
Beta strandi237 – 2415Combined sources
Helixi242 – 2498Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DK4X-ray2.60A/B1-252[»]
1G0HX-ray2.30A/B1-252[»]
1G0IX-ray2.40A/B1-252[»]
ProteinModelPortaliQ57573.
SMRiQ57573. Positions 1-252.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ57573.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 863Substrate binding1 Publication

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiarCOG01349. Archaea.
COG0483. LUCA.
InParanoidiQ57573.
KOiK01092.
OMAiSALELCY.
PhylomeDBiQ57573.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
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.

Q57573-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKWDEIGKNI AKEIEKEILP YFGRKDKSYV VGTSPSGDET EIFDKISEDI
60 70 80 90 100
ALKYLKSLNV NIVSEELGVI DNSSEWTVVI DPIDGSFNFI NGIPFFAFCF
110 120 130 140 150
GVFKNNEPYY GLTYEFLTKS FYEAYKGKGA YLNGRKIKVK DFNPNNIVIS
160 170 180 190 200
YYPSKKIDLE KLRNKVKRVR IFGAFGLEMC YVAKGTLDAV FDVRPKVRAV
210 220 230 240 250
DIASSYIICK EAGALITDEN GDELKFDLNA TDRLNIIVAN SKEMLDIILD

LL
Length:252
Mass (Da):28,578
Last modified:November 1, 1996 - v1
Checksum:i3ED5B4401075EE6E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98091.1.
PIRiE64313.

Genome annotation databases

EnsemblBacteriaiAAB98091; AAB98091; MJ_0109.
KEGGimja:MJ_0109.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98091.1.
PIRiE64313.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DK4X-ray2.60A/B1-252[»]
1G0HX-ray2.30A/B1-252[»]
1G0IX-ray2.40A/B1-252[»]
ProteinModelPortaliQ57573.
SMRiQ57573. Positions 1-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0109.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98091; AAB98091; MJ_0109.
KEGGimja:MJ_0109.

Phylogenomic databases

eggNOGiarCOG01349. Archaea.
COG0483. LUCA.
InParanoidiQ57573.
KOiK01092.
OMAiSALELCY.
PhylomeDBiQ57573.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-5062.
BRENDAi3.1.3.25. 3260.

Miscellaneous databases

EvolutionaryTraceiQ57573.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
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_METJA
AccessioniPrimary (citable) accession number: Q57573
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 119 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. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.