NRNA_THET8
ID NRNA_THET8 Reviewed; 324 AA.
AC Q5SM25;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Bifunctional oligoribonuclease and PAP phosphatase NrnA;
DE EC=3.1.-.-;
DE AltName: Full=3'(2'),5'-bisphosphate nucleotidase;
DE EC=3.1.3.7;
DE AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase;
DE Short=PAP phosphatase;
GN Name=nrnA; OrderedLocusNames=TTHA0118;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION AS AN EXONUCLEASE, FUNCTION AS A PAP PHOSPHATASE,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ASP-114.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=21087930; DOI=10.1074/jbc.m110.161596;
RA Wakamatsu T., Kim K., Uemura Y., Nakagawa N., Kuramitsu S., Masui R.;
RT "Role of RecJ-like protein with 5'-3' exonuclease activity in
RT oligo(deoxy)nucleotide degradation.";
RL J. Biol. Chem. 286:2807-2816(2011).
CC -!- FUNCTION: Bifunctional enzyme which has both oligoribonuclease and pAp-
CC phosphatase activities. Degrades short RNA and DNA oligonucleotides
CC with a length of up to 33 nucleotides, although the enzyme is most
CC active on shorter substrates, in a 5' to 3' direction. Converts 3'(2')-
CC phosphoadenosine 5'-phosphate (PAP) to AMP, has very low activity on
CC cAMP and cGMP. {ECO:0000269|PubMed:21087930}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:21087930};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21087930};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21087930};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21087930};
CC Note=Requires a divalent cation; Co(2+) > Mn(2+) >Zn(2+) > Mg(2+).
CC {ECO:0000269|PubMed:21087930};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=65 uM for ssDNA 3-mers {ECO:0000269|PubMed:21087930};
CC KM=280 uM for ssRNA 3-mers {ECO:0000269|PubMed:21087930};
CC KM=120 uM for ssDNA 6-mers {ECO:0000269|PubMed:21087930};
CC KM=270 uM for ssRNA 6-mers {ECO:0000269|PubMed:21087930};
CC KM=68 uM for ssDNA 11-mers {ECO:0000269|PubMed:21087930};
CC KM=450 uM for ssRNA 11-mers {ECO:0000269|PubMed:21087930};
CC KM=78 uM for ssDNA 21-mers {ECO:0000269|PubMed:21087930};
CC KM=470 uM for ssRNA 21-mers {ECO:0000269|PubMed:21087930};
CC KM=18 uM for PAP {ECO:0000269|PubMed:21087930};
CC Note=kcat for ss nucleic acids decreases about 5 orders of magnitude
CC as chain length increases from 3-mers to 21-mers.;
CC -!- SUBUNIT: Oligomeric. {ECO:0000269|PubMed:21087930}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth in minimal medium, possibly also
CC affected in cysteine assimilation. {ECO:0000269|PubMed:21087930}.
CC -!- SIMILARITY: Belongs to the NrnA oligoribonuclease family.
CC {ECO:0000305}.
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DR EMBL; AP008226; BAD69941.1; -; Genomic_DNA.
DR RefSeq; WP_011227723.1; NC_006461.1.
DR RefSeq; YP_143384.1; NC_006461.1.
DR AlphaFoldDB; Q5SM25; -.
DR SMR; Q5SM25; -.
DR STRING; 300852.55771500; -.
DR EnsemblBacteria; BAD69941; BAD69941; BAD69941.
DR GeneID; 3169676; -.
DR KEGG; ttj:TTHA0118; -.
DR PATRIC; fig|300852.9.peg.116; -.
DR eggNOG; COG0618; Bacteria.
DR HOGENOM; CLU_039720_0_1_0; -.
DR OMA; YTGIMTD; -.
DR PhylomeDB; Q5SM25; -.
DR SABIO-RK; Q5SM25; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR003156; DHHA1_dom.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02272; DHHA1; 1.
DR SUPFAM; SSF64182; SSF64182; 1.
PE 1: Evidence at protein level;
KW Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..324
FT /note="Bifunctional oligoribonuclease and PAP phosphatase
FT NrnA"
FT /id="PRO_0000419755"
FT MUTAGEN 114
FT /note="D->A: Decreased substrate affinity (KM 420 uM) and
FT catalytic activity for a ssDNA 6-mer."
FT /evidence="ECO:0000269|PubMed:21087930"
SQ SEQUENCE 324 AA; 35121 MW; 88D8AC7D89F21570 CRC64;
MDGNAPEPRY WEKMRLVAEV LKAVEGPIYI ATHVDPDGDA IGSSLGLYRA LKALGKEAYW
VADPPRFLRF LPKEEEYSDP VEKLPPGATL VALDSAEPSR VVGVPVEGFV INIDHHGTNP
RFGHLHVVDP SKAATAQMVK DLIDLLGVEW TAEIATPVLT GILTDTGNFR FANTTPEVLR
VAAELLGYGV KLAELTDRLQ FRPPSYFRLM GQVLSTVAFH FGGLLVTAHL PEDAGAEEDS
DDFVGLIRYV EGSVVSVFLR KREEGVKVSI RSRGGVSAQN IALKLGGGGH VPAAGATLKG
LDLDQAYERV LEAVREELTR AGYL
