PDTIR_PARDP
ID PDTIR_PARDP Reviewed; 299 AA.
AC A1AY86;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=NAD(+) hydrolase PdTIR {ECO:0000305};
DE EC=3.2.2.6 {ECO:0000269|PubMed:29395922};
DE AltName: Full=TIR domain-containing protein in P.denitrificans {ECO:0000303|PubMed:29395922};
DE Short=PdTIR {ECO:0000303|PubMed:29395922};
GN OrderedLocusNames=Pden_0113 {ECO:0000312|EMBL:ABL68230.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29395922; DOI=10.1016/j.cub.2017.12.024;
RA Essuman K., Summers D.W., Sasaki Y., Mao X., Yim A.K.Y., DiAntonio A.,
RA Milbrandt J.;
RT "TIR domain proteins are an ancient family of NAD+-consuming enzymes.";
RL Curr. Biol. 28:421-430(2018).
RN [3] {ECO:0007744|PDB:3H16}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 146-299, INTERACTION WITH HOST
RP MYD88, AND SUBUNIT.
RX PubMed=19535337; DOI=10.1074/jbc.c109.007591;
RA Chan S.L., Low L.Y., Hsu S., Li S., Liu T., Santelli E., Le Negrate G.,
RA Reed J.C., Woods V.L., Pascual J.;
RT "Molecular mimicry in innate immunity: crystal structure of a bacterial TIR
RT domain.";
RL J. Biol. Chem. 284:21386-21392(2009).
CC -!- FUNCTION: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+)
CC into ADP-D-ribose (ADPR) and nicotinamide.
CC {ECO:0000269|PubMed:29395922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000269|PubMed:29395922};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000269|PubMed:29395922};
CC -!- SUBUNIT: Homodimer (PubMed:19535337). Interacts with host MYD88
CC (PubMed:19535337). {ECO:0000269|PubMed:19535337}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
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DR EMBL; CP000489; ABL68230.1; -; Genomic_DNA.
DR PDB; 3H16; X-ray; 2.50 A; A/B/C/D=146-299.
DR PDBsum; 3H16; -.
DR AlphaFoldDB; A1AY86; -.
DR SMR; A1AY86; -.
DR STRING; 318586.Pden_0113; -.
DR PRIDE; A1AY86; -.
DR EnsemblBacteria; ABL68230; ABL68230; Pden_0113.
DR KEGG; pde:Pden_0113; -.
DR eggNOG; COG4916; Bacteria.
DR HOGENOM; CLU_086674_0_0_5; -.
DR OMA; FISHAWE; -.
DR EvolutionaryTrace; A1AY86; -.
DR Proteomes; UP000000361; Chromosome 1.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003953; F:NAD+ nucleosidase activity; IDA:UniProtKB.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0019677; P:NAD catabolic process; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR Pfam; PF13676; TIR_2; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; NAD; Reference proteome.
FT CHAIN 1..299
FT /note="NAD(+) hydrolase PdTIR"
FT /id="PRO_0000449141"
FT DOMAIN 164..297
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 173..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:3H16"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3H16"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:3H16"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:3H16"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3H16"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:3H16"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:3H16"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:3H16"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:3H16"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:3H16"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3H16"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:3H16"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:3H16"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:3H16"
SQ SEQUENCE 299 AA; 32902 MW; A6BEC1A64640F89B CRC64;
MSANDRAIET LRREIAKLQT DGAAIARKDA GIRAKLASAM AAQAKAKTAP ALRLKQAEAS
RLEKELMATS KSQADIATKI AKKQSSLSAK LVVQANEAKK ADAKAKKNQE RVSKTQEEAT
RKLEAGYRKL TLENQSLEQR LQRELSAMKP TAGPTTNADL TSAPPHDIFI SHAWEDKADF
VEALAHTLRA AGAEVWYDDF SLRPGDSLRR SIDKGLGSSR FGIVVLSTHF FKKEWPQKEL
DGLFQLESSG RSRILPIWHK VSKDEVASFS PTMADKLAFN TSTKSVDEIV ADLMAIIRD
