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O33832 (SUHB_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol-1-monophosphatase
Short name=I-1-Pase
Short name=IMPase
Short name=Inositol-1-phosphatase
EC=3.1.3.25
Gene names
Name:suhB
Ordered Locus Names:TM_1415
OrganismThermotoga maritima
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Displays a 20-fold higher rate of hydrolysis of the D isoform of inositol 1-phosphate than of the L isoform.

Catalytic activity

Myo-inositol phosphate + H2O = myo-inositol + phosphate.

Cofactor

Magnesium.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the inositol monophosphatase family.

Sequence caution

The sequence AAD36486.1 differs from that shown. Reason: Frameshift at position 22.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256Inositol-1-monophosphatase
PRO_0000142574

Regions

Region81 – 844Substrate binding By similarity

Sites

Metal binding651Magnesium 1 By similarity
Metal binding791Magnesium 1 By similarity
Metal binding791Magnesium 2 By similarity
Metal binding811Magnesium 1; via carbonyl oxygen By similarity
Metal binding821Magnesium 2 By similarity
Metal binding2011Magnesium 2 By similarity
Binding site651Substrate By similarity
Binding site1721Substrate By similarity
Binding site2011Substrate By similarity

Secondary structure

1 ............................................ 256
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O33832 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 550C15FEEA50B8DC

FASTA25628,647
        10         20         30         40         50         60 
MDRLDFSIKL LRKVGHLLMI HWGRVDNVEK KTGFKDIVTE IDREAQRMIV DEIRKFFPDE 

        70         80         90        100        110        120 
NIMAEEGIFE KGDRLWIIDP IDGTINFVHG LPNFSISLAY VENGEVKLGV VHAPALNETL 

       130        140        150        160        170        180 
YAEEGSGAFF NGERIRVSEN ASLEECVGST GSYVDFTGKF IERMEKRTRR IRILGSAALN 

       190        200        210        220        230        240 
AAYVGAGRVD FFVTWRINPW DIAAGLIIVK EAGGMVTDFS GKEANAFSKN FIFSNGLIHD 

       250 
EVVKVVNEVV EEIGGK

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the gene for beta-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima, and characterisation of the enzyme expressed in Escherichia coli."
Liebl W., Brem D., Gotschlich A.
Appl. Microbiol. Biotechnol. 50:55-64(1998) [PubMed: 9720201] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"Characterization of a tetrameric inositol monophosphatase from the hyperthermophilic bacterium Thermotoga maritima."
Chen L., Roberts M.F.
Appl. Environ. Microbiol. 65:4559-4567(1999) [PubMed: 10508089] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ001073 Genomic DNA. Translation: CAA04517.1.
AE000512 Genomic DNA. Translation: AAD36486.1. Frameshift.
PIRE72255.
T50642.
RefSeqNP_229216.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P3NX-ray2.20A/B/C/D1-256[»]
2P3VX-ray2.40A/B/C/D1-256[»]
ProteinModelPortalO33832.
SMRO33832. Positions 1-256.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID898061.
GenomeReviewsGene locus TM_1415 in contig AE000512_GR.
KEGGtma:TM1415.
NMPDRfig|243274.1.peg.1400.
PATRIC23937774. VBITheMar51294_1426.
TIGRTM_1415.

Phylogenomic databases

HOGENOMHBG730251.
OMASPRINVM.
PhylomeDBO33832.
ProtClustDBCLSK875749.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-5063.
TMAR243274:TM_1415-MONOMER.
BRENDA3.1.3.25. 6331.

Family and domain databases

InterProIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
KOK01092.
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSPR00377. IMPHPHTASES.
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSUHB_THEMA
AccessionPrimary (citable) accession number: O33832
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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