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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

  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

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi38 – 381Magnesium 3
Metal bindingi40 – 401Magnesium 3
Metal bindingi67 – 671Magnesium 1
Metal bindingi67 – 671Magnesium 3
Metal bindingi82 – 821Magnesium 1
Metal bindingi82 – 821Magnesium 2
Metal bindingi84 – 841Magnesium 1; via carbonyl oxygen
Metal bindingi85 – 851Magnesium 2
Binding sitei167 – 1671Substrate
Binding sitei172 – 1721Substrate; via amide nitrogen
Binding sitei191 – 1911Substrate
Metal bindingi200 – 2001Magnesium 2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Gluconeogenesis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-2421-MONOMER.
BRENDAi3.1.3.11. 414.
3.1.3.25. 414.
UniPathwayiUPA00138.

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 252252Fructose-1,6-bisphosphatase/inositol-1-monophosphatasePRO_0000142579Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224325.AF2372.

Structurei

Secondary structure

1
252
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2220Combined sources
Helixi26 – 294Combined sources
Beta strandi32 – 354Combined sources
Beta strandi37 – 437Combined sources
Helixi44 – 5714Combined sources
Beta strandi60 – 667Combined sources
Turni67 – 693Combined sources
Beta strandi70 – 723Combined sources
Beta strandi76 – 8510Combined sources
Helixi87 – 915Combined sources
Beta strandi98 – 10811Combined sources
Helixi109 – 1113Combined sources
Beta strandi112 – 1198Combined sources
Turni120 – 1223Combined sources
Beta strandi125 – 1295Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi147 – 1559Combined sources
Beta strandi164 – 1685Combined sources
Helixi172 – 1809Combined sources
Beta strandi183 – 1897Combined sources
Helixi198 – 21013Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi236 – 2394Combined sources
Turni241 – 2433Combined sources
Helixi244 – 2518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-252.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO30298.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni85 – 873Substrate binding

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

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

Family and domain databases

InterProiIPR000760. 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.

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
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. Positions 1-252.
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

UniPathwayiUPA00138.
BioCyciAFUL224325:GJBC-2421-MONOMER.
BRENDAi3.1.3.11. 414.
3.1.3.25. 414.

Miscellaneous databases

EvolutionaryTraceiO30298.

Family and domain databases

InterProiIPR000760. 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...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  2. "Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: comparison with bacterial and archaeal inositol monophosphatases."
    Chen L., Roberts M.F.
    Biochemistry 39:4145-4153(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS IMPASE, CATALYTIC ACTIVITY.
  3. "MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase."
    Stec B., Yang H., Johnson K.A., Chen L., Roberts M.F.
    Nat. Struct. Biol. 7:1046-1050(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS BOTH FBPASE AND IMPASE, CATALYTIC ACTIVITY, KINETIC PARAMETERS, SUBUNIT.
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  4. "Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop."
    Stieglitz K.A., Johnson K.A., Yang H., Roberts M.F., Seaton B.A., Head J.F., Stec B.
    J. Biol. Chem. 277:22863-22874(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH I-1-P; FBP; F-6-P AND METAL IONS, FUNCTION AS BOTH FBPASE AND IMPASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, ENZYME REGULATION, COFACTOR.

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: January 20, 2016
This is version 117 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.