Reviewed, UniProtKB/Swiss-Prot P0ADG4 (SUHB_ECOLI)

Names and origin

Protein names

Recommended name:
    Inositol-1-monophosphatase
      Short name=IMPase
      Short name=Inositol-1-phosphatase
      Short name=I-1-Pase
    EC=3.1.3.25

Gene names

Name:	suhB
Synonyms:	ssyA
Ordered Locus Names:	b2533, JW2517

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	267 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Molecular function	inositol-1(or 4)-monophosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 267

267

Inositol-1-monophosphatase

PRO_0000142559

Regions

Region

86 – 89

4

Substrate binding By similarity

Sites

Metal binding

67

1

Magnesium 1 By similarity

Metal binding

84

1

Magnesium 1 By similarity

Metal binding

84

1

Magnesium 2 By similarity

Metal binding

86

1

Magnesium 1; via carbonyl oxygen By similarity

Metal binding

87

1

Magnesium 2 By similarity

Metal binding

212

1

Magnesium 2 By similarity

Binding site

67

1

Substrate By similarity

Binding site

183

1

Substrate By similarity

Binding site

212

1

Substrate By similarity

Experimental info

Sequence conflict

141

1

R → L in AAA67506. Ref.1

Secondary structure

1

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267

Helix Strand Turn

Details...

Helix

2 – 14

13

Helix

18 – 23

6

Helix

38 – 58

21

Beta strand

62 – 67

6

Beta strand

76 – 87

12

Helix

90 – 94

5

Beta strand

100 – 107

8

Beta strand

111 – 118

8

Turn

119 – 122

4

Beta strand

123 – 128

6

Beta strand

152 – 155

4

Helix

162 – 164

3

Helix

165 – 171

7

Helix

176 – 178

3

Beta strand

181 – 184

4

Helix

188 – 196

9

Helix

210 – 213

4

Helix

218 – 222

5

Turn

236 – 238

3

Helix

247 – 255

9

Turn

256 – 259

4

Sequences

	Sequence		Length	Mass (Da)
	P0ADG4-1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 8FEC3508BD111301	FASTA	267	29,172
	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

References

	« Hide 'large scale' referencesShow '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: 2138605] [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. , 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: 9205837] [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: 9278503] [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: 16738553] [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: 8002619] [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: 10747806] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M34828 Genomic DNA. Translation: AAA67506.1.
U00096 Genomic DNA. Translation: AAC75586.1.
AP009048 Genomic DNA. Translation: BAA16427.1.

PIR

D65030.

RefSeq

AP_003119.1.
NP_417028.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QFL	X-ray	1.90	A	1-267	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0ADG4.

2-D gel databases

SWISS-2DPAGE

P0ADG4.

Genome annotation databases

GeneID

947285.

GenomeReviews

Gene locus JW2517 in contig AP009048_GR.
Gene locus b2533 in contig U00096_GR.

KEGG

ecj:JW2517.
eco:b2533.

Organism-specific databases

EchoBASE

EB0976.

EcoGene

EG10983. suhB.

CMR

Search...

Phylogenomic databases

HOGENOM

P0ADG4.

OMA

KGINDYV.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10983-MON.
MetaCyc:EG10983-MON.

Gene expression databases

Genevestigator

P0ADG4.

Family and domain databases

InterPro

IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]

PANTHER

PTHR20854. Inositol_P. 1 hit.

Pfam

PF00459. Inositol_P. 1 hit.
[Graphical view]

PRINTS

PR00377. IMPHPHTASES.

ProDom

PD023420. Inositol_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SUHB_ECOLI

Accession

Primary (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:	November 3, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)