Reviewed, UniProtKB/Swiss-Prot P96112 (SURE_THEMA)

Names and origin

Protein names

Recommended name:
    5'-nucleotidase surE
    EC=3.1.3.5
Alternative name(s):
    Nucleoside 5'-monophosphate phosphohydrolase

Gene names

Name:	surE
Ordered Locus Names:	TM_1662

Organism

Thermotoga maritima [Complete proteome] [HAMAP]

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	247 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Nucleotidase that preferentially dephosphorylates 5'-GMP and 5'-AMP. HAMAP MF_00060
Catalytic activity	A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP MF_00060
Cofactor	Binds 1 magnesium ion per subunit. In contrast to other surE homologs, is essentially inactive with other divalent cations. Ref.3
Enzyme regulation	Inhibited by vanadate and tungstate. HAMAP MF_00060
Subunit structure	Homodimer and possibly homotetramer. Ref.4
Subcellular location	Cytoplasm Potential.
Sequence similarities	Belongs to the surE nucleotidase family.
Caution	Was originally annotated as an acid phosphatase (EC 3.1.3.2).
Biophysicochemical properties	Kinetic parameters: KM=31.5 mM for pNPP (at 76 degrees Celsius) HAMAP MF_00060 Vmax=51.6 µmol/min/mg enzyme with pNPP as substrate (at 76 degrees Celsius) pH dependence: Optimum pH is 5.5-6.2. Temperature dependence: Optimum temperature is 80 degrees Celsius. Active up to 95 degrees Celsius.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	5'-nucleotidase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide 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 – 247

247

5'-nucleotidase surE HAMAP MF_00060

PRO_0000111846

Sites

Metal binding

8

1

Magnesium HAMAP MF_00060

Metal binding

9

1

Magnesium HAMAP MF_00060

Metal binding

39

1

Magnesium HAMAP MF_00060

Metal binding

95

1

Magnesium HAMAP MF_00060

Experimental info

Mutagenesis

8

1

D → N: Loss of activity.

Mutagenesis

9

1

D → N: Loss of activity.

Mutagenesis

127

1

S → A: Loss of activity.

Secondary structure

1

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247

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

14 – 24

11

Beta strand

27 – 36

10

Beta strand

53 – 59

7

Beta strand

62 – 69

8

Helix

71 – 81

11

Beta strand

88 – 97

10

Helix

101 – 106

6

Helix

108 – 118

11

Beta strand

123 – 129

7

Beta strand

131 – 133

3

Helix

136 – 147

12

Helix

152 – 154

3

Beta strand

160 – 165

6

Beta strand

172 – 175

4

Beta strand

182 – 191

10

Beta strand

197 – 206

10

Beta strand

211 – 214

4

Helix

215 – 220

6

Beta strand

223 – 229

7

Helix

236 – 245

10

Sequences

	Sequence		Length	Mass (Da)
	P96112-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 09F4A68A80C0B241	FASTA	247	28,075
	10 20 30 40 50 60 MRILVTNDDG IQSKGIIVLA ELLSEEHEVF VVAPDKERSA TGHSITIHVP LWMKKVFISE 70 80 90 100 110 120 RVVAYSTTGT PADCVKLAYN VVMDKRVDLI VSGVNRGPNM GMDILHSGTV SGAMEGAMMN 130 140 150 160 170 180 IPSIAISSAN YESPDFEGAA RFLIDFLKEF DFSLLDPFTM LNINVPAGEI KGWRFTRQSR 190 200 210 220 230 240 RRWNDYFEER VSPFGEKYYW MMGEVIEDDD RDDVDYKAVR EGYVSITPIH PFLTNEQCLK KLREVYD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"A survey of polypeptide deformylase function throughout the eubacterial lineage." Mazel D., Coic E., Blanchard S., Saurin W., Marliere P. J. Mol. Biol. 266:939-949(1997) [PubMed: 9086272] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 156-247.
[3]	"Structure and function of an archaeal homolog of survival protein E (SurEalpha): an acid phosphatase with purine nucleotide specificity." Mura C., Katz J.E., Clarke S.G., Eisenberg D. J. Mol. Biol. 326:1559-1575(2003) [PubMed: 12595266] [Abstract] Cited for: COFACTOR.
[4]	"Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase." Zhang R.-G., Skarina T., Katz J.E., Beasley S., Khachatryan A., Vyas S., Arrowsmith C.H., Clarke S., Edwards A., Joachimiak A., Savchenko A. Structure 9:1095-1106(2001) [PubMed: 11709173] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), CHARACTERIZATION, SUBUNIT, MUTAGENESIS.
[5]	"Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family." Lee J.Y., Kwak J.E., Moon J., Eom S.H., Liong E.C., Pedelacq J.-D., Berendzen J., Suh S.W. Nat. Struct. Biol. 8:789-794(2001) [PubMed: 11524683] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), CHARACTERIZATION.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE000512 Genomic DNA. Translation: AAD36729.1.
Y10306 Genomic DNA. Translation: CAA71355.1.

PIR

D72224.

RefSeq

NP_229462.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ILV	X-ray	2.00	A/B	1-247	[»]
1J9J	X-ray	1.90	A/B	1-247	[»]
1J9K	X-ray	2.10	A/B	1-247	[»]
1J9L	X-ray	1.90	A/B	1-247	[»]

ModBase

Search...

Genome annotation databases

GeneID

897339.

GenomeReviews

Gene locus TM_1662 in contig AE000512_GR.

KEGG

tma:TM1662.

NMPDR

fig|243274.1.peg.1646.

TIGR

TM_1662.

Phylogenomic databases

HOGENOM

P96112.

OMA

SINIPIK.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1662-MON.

BRENDA

3.1.3.5. 16699.

Family and domain databases

HAMAP

MF_00060.
[Tree]

InterPro

IPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]

Gene3D

G3DSA:3.40.1210.10. SurE-like_Pase/nucleotidase. 1 hit.

Pfam

PF01975. SurE. 1 hit.
[Graphical view]

ProDom

PD005378. SurE. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00087. surE. 1 hit.

ProtoNet

Search...

Entry information

Entry name

SURE_THEMA

Accession

Primary (citable) accession number: P96112

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	November 3, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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