SURE_THEMA
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 03-AUG-2022, entry version 151.
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; Thermotogae; Thermotogales; 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}.
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DR EMBL; AE000512; AAD36729.1; -; Genomic_DNA.
DR EMBL; Y10306; CAA71355.1; -; Genomic_DNA.
DR PIR; D72224; D72224.
DR RefSeq; NP_229462.1; NC_000853.1.
DR RefSeq; WP_004082178.1; NZ_CP011107.1.
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 PDBsum; 1ILV; -.
DR PDBsum; 1J9J; -.
DR PDBsum; 1J9K; -.
DR PDBsum; 1J9L; -.
DR AlphaFoldDB; P96112; -.
DR SMR; P96112; -.
DR STRING; 243274.THEMA_05935; -.
DR DNASU; 897339; -.
DR EnsemblBacteria; AAD36729; AAD36729; TM_1662.
DR KEGG; tma:TM1662; -.
DR eggNOG; COG0496; Bacteria.
DR InParanoid; P96112; -.
DR OMA; DCVHIAL; -.
DR OrthoDB; 1909278at2; -.
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 GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046050; P:UMP catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.1210.10; -; 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 PANTHER; PTHR30457; PTHR30457; 1.
DR Pfam; PF01975; SurE; 1.
DR SUPFAM; SSF64167; SSF64167; 1.
DR TIGRFAMs; TIGR00087; surE; 1.
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..80
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
