ID SURE_THEMA Reviewed; 247 AA. AC P96112; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 02-SEP-2026, entry version 165. DE RecName: Full=5'-nucleotidase SurE; DE EC=3.1.3.5; DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase; GN Name=surE; OrderedLocusNames=TM_1662; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales; OC Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 156-247. RX PubMed=9086272; DOI=10.1006/jmbi.1996.0835; RA Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.; RT "A survey of polypeptide deformylase function throughout the eubacterial RT lineage."; RL J. Mol. Biol. 266:939-949(1997). RN [3] RP COFACTOR. RX PubMed=12595266; DOI=10.1016/s0022-2836(03)00056-1; RA Mura C., Katz J.E., Clarke S.G., Eisenberg D.; RT "Structure and function of an archaeal homolog of survival protein E RT (SurEalpha): an acid phosphatase with purine nucleotide specificity."; RL J. Mol. Biol. 326:1559-1575(2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), CHARACTERIZATION, SUBUNIT, AND RP MUTAGENESIS. RX PubMed=11709173; DOI=10.1016/s0969-2126(01)00675-x; RA Zhang R.-G., Skarina T., Katz J.E., Beasley S., Khachatryan A., Vyas S., RA Arrowsmith C.H., Clarke S., Edwards A., Joachimiak A., Savchenko A.; RT "Structure of Thermotoga maritima stationary phase survival protein SurE: a RT novel acid phosphatase."; RL Structure 9:1095-1106(2001). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND CHARACTERIZATION. RX PubMed=11524683; DOI=10.1038/nsb0901-789; RA Lee J.Y., Kwak J.E., Moon J., Eom S.H., Liong E.C., Pedelacq J.-D., RA Berendzen J., Suh S.W.; RT "Crystal structure and functional analysis of the SurE protein identify a RT novel phosphatase family."; RL Nat. Struct. Biol. 8:789-794(2001). CC -!- FUNCTION: Nucleotidase that preferentially dephosphorylates 5'-GMP and CC 5'-AMP. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:12595266}; CC Note=Binds 1 Mg(2+) ion per subunit. In contrast to other surE CC homologs, is essentially inactive with other divalent cations. CC {ECO:0000269|PubMed:12595266}; CC -!- ACTIVITY REGULATION: Inhibited by vanadate and tungstate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=31.5 mM for pNPP (at 76 degrees Celsius); CC Vmax=51.6 umol/min/mg enzyme with pNPP as substrate (at 76 degrees CC Celsius); CC pH dependence: CC Optimum pH is 5.5-6.2.; CC Temperature dependence: CC Optimum temperature is 80 degrees Celsius. Active up to 95 degrees CC Celsius.; CC -!- SUBUNIT: Homodimer and possibly homotetramer. CC {ECO:0000269|PubMed:11709173}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the SurE nucleotidase family. {ECO:0000305}. CC -!- CAUTION: Was originally annotated as an acid phosphatase (EC 3.1.3.2). CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000512; AAD36729.1; -; Genomic_DNA. DR EMBL; Y10306; CAA71355.1; -; Genomic_DNA. DR PIR; D72224; D72224. DR RefSeq; WP_004082178.1; NC_000853.1. DR PDB; 1ILV; X-ray; 2.00 A; A/B=1-247. DR PDB; 1J9J; X-ray; 1.90 A; A/B=1-247. DR PDB; 1J9K; X-ray; 2.10 A; A/B=1-247. DR PDB; 1J9L; X-ray; 1.90 A; A/B=1-247. DR AlphaFoldDB; P96112; -. DR SMR; P96112; -. DR STRING; 243274.TM_1662; -. DR PaxDb; 243274-TM_1662; -. DR DNASU; 897339; -. DR EnsemblBacteria; AAD36729; AAD36729; TM_1662. DR KEGG; tma:TM1662; -. DR KEGG; tmi:THEMA_05935; -. DR KEGG; tmm:Tmari_1671; -. DR KEGG; tmw:THMA_1703; -. DR eggNOG; COG0496; Bacteria. DR InParanoid; P96112; -. DR OrthoDB; 9780815at2; -. DR EvolutionaryTrace; P96112; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008254; F:3'-nucleotidase activity; IBA:GO_Central. DR GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central. DR GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR FunFam; 3.40.1210.10:FF:000001; 5'/3'-nucleotidase SurE; 1. DR Gene3D; 3.40.1210.10; Survival protein SurE-like phosphatase/nucleotidase; 1. DR HAMAP; MF_00060; SurE; 1. DR InterPro; IPR030048; SurE. DR InterPro; IPR002828; SurE-like_Pase/nucleotidase. DR InterPro; IPR036523; SurE-like_sf. DR NCBIfam; NF001490; PRK00346.1-4; 1. DR NCBIfam; NF001492; PRK00346.2-2; 1. DR NCBIfam; NF010545; PRK13935.1; 1. DR NCBIfam; TIGR00087; surE; 1. DR PANTHER; PTHR30457; 5'-NUCLEOTIDASE SURE; 1. DR PANTHER; PTHR30457:SF12; 5'_3'-NUCLEOTIDASE SURE; 1. DR Pfam; PF01975; SurE; 1. DR SUPFAM; SSF64167; SurE-like; 1. DR PDBsum; 1ILV; -. DR PDBsum; 1J9J; -. DR PDBsum; 1J9K; -. DR PDBsum; 1J9L; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Hydrolase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..247 FT /note="5'-nucleotidase SurE" FT /id="PRO_0000111846" FT BINDING 8 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 9 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 39 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 95 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT MUTAGEN 8 FT /note="D->N: Loss of activity." FT /evidence="ECO:0000269|PubMed:11709173" FT MUTAGEN 9 FT /note="D->N: Loss of activity." FT /evidence="ECO:0000269|PubMed:11709173" FT MUTAGEN 127 FT /note="S->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:11709173" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:1J9J" FT HELIX 14..23 FT /evidence="ECO:0007829|PDB:1J9J" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 27..36 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 59..69 FT /evidence="ECO:0007829|PDB:1J9J" FT HELIX 71..77 FT /evidence="ECO:0007829|PDB:1J9J" FT HELIX 78..82 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 88..97 FT /evidence="ECO:0007829|PDB:1J9J" FT HELIX 101..106 FT /evidence="ECO:0007829|PDB:1J9J" FT HELIX 108..118 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 123..129 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:1J9J" FT HELIX 136..149 FT /evidence="ECO:0007829|PDB:1J9J" FT HELIX 152..154 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 172..175 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 182..191 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 197..206 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:1J9J" FT HELIX 215..220 FT /evidence="ECO:0007829|PDB:1J9J" FT STRAND 223..229 FT /evidence="ECO:0007829|PDB:1J9J" FT HELIX 236..245 FT /evidence="ECO:0007829|PDB:1J9J" SQ SEQUENCE 247 AA; 28075 MW; 09F4A68A80C0B241 CRC64; MRILVTNDDG IQSKGIIVLA ELLSEEHEVF VVAPDKERSA TGHSITIHVP LWMKKVFISE RVVAYSTTGT PADCVKLAYN VVMDKRVDLI VSGVNRGPNM GMDILHSGTV SGAMEGAMMN IPSIAISSAN YESPDFEGAA RFLIDFLKEF DFSLLDPFTM LNINVPAGEI KGWRFTRQSR RRWNDYFEER VSPFGEKYYW MMGEVIEDDD RDDVDYKAVR EGYVSITPIH PFLTNEQCLK KLREVYD //