NRNA_MYCTU
ID NRNA_MYCTU Reviewed; 336 AA.
AC P71615; F2GL96; L0TDH8;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 25-MAY-2022, entry version 118.
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;
DE AltName: Full=nanoRNase;
GN Name=nrnA; OrderedLocusNames=Rv2837c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION AS AN OLIGORIBONUCLEASE, FUNCTION AS A PAP PHOSPHATASE, AND
RP COFACTOR.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22114320; DOI=10.1261/rna.029132.111;
RA Postic G., Danchin A., Mechold U.;
RT "Characterization of NrnA homologs from Mycobacterium tuberculosis and
RT Mycoplasma pneumoniae.";
RL RNA 18:155-165(2012).
RN [4]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
CC -!- FUNCTION: Bifunctional enzyme which has both oligoribonuclease and pAp-
CC phosphatase activities. Degrades RNA oligonucleotides with a length of
CC 5 nucleotides and shorter, with a preference for 2-mers. Also degrades
CC 24-mers. Converts 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP.
CC {ECO:0000269|PubMed:22114320}.
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:22114320};
CC -!- MISCELLANEOUS: In accordance with its dual activities, is able to
CC complement both orn and cysQ mutants in E.coli.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the NrnA oligoribonuclease family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45638.1; -; Genomic_DNA.
DR PIR; H70693; H70693.
DR RefSeq; NP_217353.1; NC_000962.3.
DR RefSeq; WP_003414507.1; NZ_NVQJ01000006.1.
DR PDB; 5CET; X-ray; 2.00 A; A=10-336.
DR PDB; 5JJU; X-ray; 2.31 A; A/B=10-336.
DR PDBsum; 5CET; -.
DR PDBsum; 5JJU; -.
DR AlphaFoldDB; P71615; -.
DR SMR; P71615; -.
DR STRING; 83332.Rv2837c; -.
DR PaxDb; P71615; -.
DR DNASU; 888920; -.
DR GeneID; 45426824; -.
DR GeneID; 888920; -.
DR KEGG; mtu:Rv2837c; -.
DR PATRIC; fig|83332.111.peg.3155; -.
DR TubercuList; Rv2837c; -.
DR eggNOG; COG0618; Bacteria.
DR InParanoid; P71615; -.
DR OMA; YTGIMTD; -.
DR PhylomeDB; P71615; -.
DR BRENDA; 3.1.3.7; 3445.
DR BRENDA; 3.1.4.59; 3445.
DR Proteomes; UP000001584; 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 3D-structure; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..336
FT /note="Bifunctional oligoribonuclease and PAP phosphatase
FT NrnA"
FT /id="PRO_0000419753"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 46..61
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:5CET"
FT TURN 182..186
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5CET"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5CET"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:5CET"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:5CET"
SQ SEQUENCE 336 AA; 35415 MW; 18B0A844A4BE6DB2 CRC64;
MTTIDPRSEL VDGRRRAGAR VDAVGAAALL SAAARVGVVC HVHPDADTIG AGLALALVLD
GCGKRVEVSF AAPATLPESL RSLPGCHLLV RPEVMRRDVD LVVTVDIPSV DRLGALGDLT
DSGRELLVID HHASNDLFGT ANFIDPSADS TTTMVAEILD AWGKPIDPRV AHCIYAGLAT
DTGSFRWASV RGYRLAARLV EIGVDNATVS RTLMDSHPFT WLPLLSRVLG SAQLVSEAVG
GRGLVYVVVD NREWVAARSE EVESIVDIVR TTQQAEVAAV FKEVEPHRWS VSMRAKTVNL
AAVASGFGGG GHRLAAGYTT TGSIDDAVAS LRAALG
