Reviewed, UniProtKB/Swiss-Prot O33832 (SUHB_THEMA)

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
Ordered Locus Names:	TM_1415

Organism

Thermotoga maritima [Complete proteome] [HAMAP]

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

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 – 256

256

Inositol-1-monophosphatase

PRO_0000142574

Regions

Region

81 – 84

4

Substrate binding By similarity

Sites

Metal binding

65

1

Magnesium 1 By similarity

Metal binding

79

1

Magnesium 1 By similarity

Metal binding

79

1

Magnesium 2 By similarity

Metal binding

81

1

Magnesium 1; via carbonyl oxygen By similarity

Metal binding

82

1

Magnesium 2 By similarity

Metal binding

201

1

Magnesium 2 By similarity

Binding site

65

1

Substrate By similarity

Binding site

172

1

Substrate By similarity

Binding site

201

1

Substrate By similarity

Secondary structure

1

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256

Helix Strand Turn

Details...

Helix

2 – 21

20

Beta strand

29 – 38

10

Helix

40 – 56

17

Beta strand

61 – 67

7

Beta strand

73 – 82

10

Helix

84 – 89

6

Beta strand

95 – 102

8

Beta strand

105 – 113

9

Turn

114 – 117

4

Beta strand

118 – 123

6

Turn

124 – 126

3

Beta strand

127 – 130

4

Helix

143 – 145

3

Beta strand

147 – 150

4

Helix

156 – 164

9

Turn

165 – 167

3

Beta strand

168 – 173

6

Helix

177 – 185

9

Beta strand

190 – 196

7

Helix

199 – 211

13

Beta strand

215 – 217

3

Beta strand

221 – 223

3

Beta strand

229 – 234

6

Beta strand

236 – 238

3

Helix

239 – 253

15

Sequences

	Sequence		Length	Mass (Da)
	O33832-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 550C15FEEA50B8DC	FASTA	256	28,647
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

PIR

E72255.
T50642.

RefSeq

NP_229216.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2P3N	X-ray	2.20	A/B/C/D	1-256	[»]
2P3V	X-ray	2.40	A/B/C/D	1-256	[»]

ModBase

Search...

Genome annotation databases

GeneID

898061.

GenomeReviews

Gene locus TM_1415 in contig AE000512_GR.

KEGG

tma:TM1415.

NMPDR

fig|243274.1.peg.1400.

TIGR

TM_1415.

Phylogenomic databases

HOGENOM

HBG730251.

OMA

KEANAFS.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-5063.
TMAR243274:TM_1415-MONOMER.

BRENDA

3.1.3.25. 16699.

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.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

SUHB_THEMA

Accession

Primary (citable) accession number: O33832

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	January 19, 2010
This is version 70 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)