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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)DescriptionActionsGraphical viewLength
Metal bindingi65Magnesium 12 Publications1
Metal bindingi81Magnesium 12 Publications1
Metal bindingi81Magnesium 22 Publications1
Metal bindingi83Magnesium 1; via carbonyl oxygen2 Publications1
Metal bindingi84Magnesium 22 Publications1
Binding sitei170Substrate1 Publication1
Binding sitei175Substrate; via amide nitrogen1 Publication1
Binding sitei194Substrate1 Publication1
Metal bindingi201Magnesium 22 Publications1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001425801 – 252Fructose-1,6-bisphosphatase/inositol-1-monophosphataseAdd BLAST252

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi243232.MJ_0109.

Structurei

Secondary structure

1252
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 18Combined sources16
Helixi19 – 21Combined sources3
Turni25 – 27Combined sources3
Beta strandi30 – 34Combined sources5
Turni35 – 37Combined sources3
Beta strandi38 – 41Combined sources4
Helixi42 – 55Combined sources14
Helixi56 – 58Combined sources3
Beta strandi60 – 64Combined sources5
Helixi65 – 67Combined sources3
Beta strandi68 – 70Combined sources3
Beta strandi75 – 84Combined sources10
Helixi86 – 90Combined sources5
Beta strandi97 – 115Combined sources19
Helixi116 – 118Combined sources3
Beta strandi120 – 125Combined sources6
Turni126 – 128Combined sources3
Beta strandi129 – 132Combined sources4
Helixi144 – 146Combined sources3
Beta strandi148 – 152Combined sources5
Beta strandi155 – 157Combined sources3
Helixi159 – 165Combined sources7
Beta strandi167 – 169Combined sources3
Helixi175 – 183Combined sources9
Beta strandi188 – 192Combined sources5
Helixi199 – 210Combined sources12
Turni211 – 213Combined sources3
Beta strandi215 – 217Combined sources3
Beta strandi219 – 223Combined sources5
Beta strandi237 – 241Combined sources5
Helixi242 – 249Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ57573.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni84 – 86Substrate binding1 Publication3

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-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.

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.
RefSeqiWP_010869601.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB98091; AAB98091; MJ_0109.
GeneIDi1450950.
KEGGimja:MJ_0109.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98091.1.
PIRiE64313.
RefSeqiWP_010869601.1. NC_000909.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi243232.MJ_0109.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98091; AAB98091; MJ_0109.
GeneIDi1450950.
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-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_METJA
AccessioniPrimary (citable) accession number: Q57573
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 122 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.