SURE1_PYRAE
ID SURE1_PYRAE Reviewed; 266 AA.
AC Q8ZU79;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=5'-nucleotidase SurE 1 {ECO:0000255|HAMAP-Rule:MF_00060};
DE EC=3.1.3.5 {ECO:0000255|HAMAP-Rule:MF_00060, ECO:0000269|PubMed:12595266};
DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase 1 {ECO:0000255|HAMAP-Rule:MF_00060};
GN Name=surE1; OrderedLocusNames=PAE2908;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND TEMPERATURE DEPENDENCE.
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).
CC -!- FUNCTION: Nucleotidase that shows the greatest phosphatase activity on
CC purine (deoxy)nucleoside 5'-monophosphates, particularly the substrates
CC 5'-GMP, 5'-AMP and 2'-deoxy-5'-AMP. {ECO:0000269|PubMed:12595266}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00060,
CC ECO:0000269|PubMed:12595266};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-
CC deoxyribonucleoside + phosphate; Xref=Rhea:RHEA:36167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18274, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:65317; Evidence={ECO:0000269|PubMed:12595266};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GMP + H2O = guanosine + phosphate; Xref=Rhea:RHEA:27714,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:12595266};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + H2O = adenosine + phosphate; Xref=Rhea:RHEA:29375,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:12595266};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dAMP + H2O = 2'-deoxyadenosine + phosphate;
CC Xref=Rhea:RHEA:29371, ChEBI:CHEBI:15377, ChEBI:CHEBI:17256,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58245;
CC Evidence={ECO:0000269|PubMed:12595266};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:12595266};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12595266};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12595266};
CC Note=Binds 1 divalent metal cation per subunit. Most active with
CC Co(2+), and may utilize Mg(2+) or Mn(2+), though with less activity.
CC {ECO:0000269|PubMed:12595266};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is above 90 degrees Celsius.
CC {ECO:0000269|PubMed:12595266};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12595266}.
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; AE009441; AAL64529.1; -; Genomic_DNA.
DR PDB; 1L5X; X-ray; 2.00 A; A/B=1-266.
DR PDBsum; 1L5X; -.
DR AlphaFoldDB; Q8ZU79; -.
DR SMR; Q8ZU79; -.
DR STRING; 178306.PAE2908; -.
DR EnsemblBacteria; AAL64529; AAL64529; PAE2908.
DR KEGG; pai:PAE2908; -.
DR PATRIC; fig|178306.9.peg.2175; -.
DR eggNOG; arCOG02303; Archaea.
DR HOGENOM; CLU_045192_1_3_2; -.
DR InParanoid; Q8ZU79; -.
DR OMA; DCVHIAL; -.
DR EvolutionaryTrace; Q8ZU79; -.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050484; F:GMP 5'-nucleotidase activity; IEA:RHEA.
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 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; Cobalt; Cytoplasm; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..266
FT /note="5'-nucleotidase SurE 1"
FT /id="PRO_0000111869"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT BINDING 9
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT BINDING 39
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT BINDING 93
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00060"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1L5X"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:1L5X"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1L5X"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:1L5X"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1L5X"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1L5X"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:1L5X"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:1L5X"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:1L5X"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1L5X"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:1L5X"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1L5X"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1L5X"
FT HELIX 139..159
FT /evidence="ECO:0007829|PDB:1L5X"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1L5X"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1L5X"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1L5X"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:1L5X"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:1L5X"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:1L5X"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:1L5X"
FT HELIX 252..266
FT /evidence="ECO:0007829|PDB:1L5X"
SQ SEQUENCE 266 AA; 28845 MW; 292677D5D59149D0 CRC64;
MKILVTNDDG VHSPGLRLLY QFALSLGDVD VVAPESPKSA TGLGITLHKP LRMYEVDLCG
FRAIATSGTP SDTVYLATFG LGRKYDIVLS GINLGDNTSL QVILSSGTLG AAFQAALLGI
PALAYSAYLE NWNELLNNKE AVEIMGAVVS STASYVLKNG MPQGVDVISV NFPRRLGRGV
RAKLVKAAKL RYAQQVVERV DPRGVRYYWL YGRDLAPEPE TDVYVVLKEG GIAITPLTLN
LNAVDAHREV DMDSLNRMVE YINASL
