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P0ADG4 (SUHB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:ssyA
Ordered Locus Names:b2533, JW2517
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Magnesium.

Subunit structure

Monomer.

Sequence similarities

Belongs to the inositol monophosphatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 267267Inositol-1-monophosphatase
PRO_0000142559

Regions

Region86 – 894Substrate binding By similarity

Sites

Metal binding671Magnesium 1 By similarity
Metal binding841Magnesium 1 By similarity
Metal binding841Magnesium 2 By similarity
Metal binding861Magnesium 1; via carbonyl oxygen By similarity
Metal binding871Magnesium 2 By similarity
Metal binding2121Magnesium 2 By similarity
Binding site671Substrate By similarity
Binding site1831Substrate By similarity
Binding site2121Substrate By similarity

Experimental info

Sequence conflict1411R → L in AAA67506. Ref.1

Secondary structure

1 ............................................... 267
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ADG4 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 8FEC3508BD111301

FASTA26729,172
        10         20         30         40         50         60 
MHPMLNIAVR AARKAGNLIA KNYETPDAVE ASQKGSNDFV TNVDKAAEAV IIDTIRKSYP 

        70         80         90        100        110        120 
QHTIITEESG ELEGTDQDVQ WVIDPLDGTT NFIKRLPHFA VSIAVRIKGR TEVAVVYDPM 

       130        140        150        160        170        180 
RNELFTATRG QGAQLNGYRL RGSTARDLDG TILATGFPFK AKQYATTYIN IVGKLFNECA 

       190        200        210        220        230        240 
DFRRTGSAAL DLAYVAAGRV DGFFEIGLRP WDFAAGELLV REAGGIVSDF TGGHNYMLTG 

       250        260 
NIVAGNPRVV KAMLANMRDE LSDALKR

« Hide

References

« Hide 'large scale' references
[1]"A mutation that enhances synthesis of sigma 32 and suppresses temperature-sensitive growth of the rpoH15 mutant of Escherichia coli."
Yano R., Nagai H., Shiba K., Yura T.
J. Bacteriol. 172:2124-2130(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Inositol monophosphatase activity from the Escherichia coli suhB gene product."
Matsuhisa A., Suzuki N., Noda T., Shiba K.
J. Bacteriol. 177:200-205(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"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: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M34828 Genomic DNA. Translation: AAA67506.1.
U00096 Genomic DNA. Translation: AAC75586.1.
AP009048 Genomic DNA. Translation: BAA16427.1.
PIRD65030.
RefSeqNP_417028.1. NC_000913.2.
YP_490761.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QFLX-ray1.90A1-267[»]
ProteinModelPortalP0ADG4.
SMRP0ADG4. Positions 1-262.
ModBaseSearch...

Protein-protein interaction databases

IntActP0ADG4. 5 interactions.
STRING511145.b2533.

2D gel databases

SWISS-2DPAGEP0ADG4.

Proteomic databases

PaxDbP0ADG4.
PRIDEP0ADG4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75586; AAC75586; b2533.
BAA16427; BAA16427; BAA16427.
GeneID12931606.
947285.
KEGGecj:Y75_p2486.
eco:b2533.
PATRIC32120463. VBIEscCol129921_2634.

Organism-specific databases

EchoBASEEB0976.
EcoGeneEG10983. suhB.

Phylogenomic databases

eggNOGCOG0483.
HOGENOMHOG000282238.
KOK01092.
OMAKGINDYV.
ProtClustDBPRK10757.

Enzyme and pathway databases

BioCycEcoCyc:EG10983-MONOMER.
ECOL316407:JW2517-MONOMER.
MetaCyc:EG10983-MONOMER.

Gene expression databases

GenevestigatorP0ADG4.

Family and domain databases

InterProIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
IPR022337. Inositol_monophosphatase_SuhB.
[Graphical view]
PANTHERPTHR20854. PTHR20854. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSPR00377. IMPHPHTASES.
PR01959. SBIMPHPHTASE.
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ADG4.

Entry information

Entry nameSUHB_ECOLI
AccessionPrimary (citable) accession number: P0ADG4
Secondary accession number(s): P22783, P77511, Q8X2E6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents