TIR_BRADI
ID TIR_BRADI Reviewed; 224 AA.
AC I1GTC2;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=TIR-only protein {ECO:0000303|PubMed:31439793};
DE Short=BdTIR {ECO:0000303|PubMed:31439793};
DE AltName: Full=NAD(+) hydrolase TIR;
DE EC=3.2.2.6 {ECO:0000269|PubMed:31439793};
DE AltName: Full=NADP(+) hydrolase TIR {ECO:0000305};
DE EC=3.2.2.- {ECO:0000269|PubMed:31439793};
GN ORFNames=BRADI_1g24377v3 {ECO:0000312|EMBL:KQK15683.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Bd21;
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31439793; DOI=10.1126/science.aax1771;
RA Wan L., Essuman K., Anderson R.G., Sasaki Y., Monteiro F., Chung E.H.,
RA Osborne Nishimura E., DiAntonio A., Milbrandt J., Dangl J.L.,
RA Nishimura M.T.;
RT "TIR domains of plant immune receptors are NAD+-cleaving enzymes that
RT promote cell death.";
RL Science 365:799-803(2019).
RN [3]
RP FUNCTION.
RX PubMed=34853457; DOI=10.1038/s41586-021-04098-7;
RA Ofir G., Herbst E., Baroz M., Cohen D., Millman A., Doron S., Tal N.,
RA Malheiro D.B.A., Malitsky S., Amitai G., Sorek R.;
RT "Antiviral activity of bacterial TIR domains via immune signalling
RT molecules.";
RL Nature 600:116-120(2021).
CC -!- FUNCTION: Acts as a NAD(+) hydrolase (NADase): in response to
CC activation, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and
CC nicotinamide; NAD(+) cleavage triggering a defense system that promotes
CC cell death (PubMed:31439793). In addition to ADPR, also generates a
CC cyclization variant of cyclic ADPR (cADPR), termed v-cADPR, for which
CC the cyclizing bond is unknown (PubMed:31439793). Also able to hydrolyze
CC NADP(+), but not other NAD(+)-related molecules (PubMed:31439793). v-
CC cADPR activates ThsA, an NAD(+) hydrolase in B.cereus
CC (PubMed:34853457). {ECO:0000269|PubMed:31439793,
CC ECO:0000269|PubMed:34853457}.
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:31439793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000269|PubMed:31439793};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) +
CC nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58673; Evidence={ECO:0000269|PubMed:31439793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850;
CC Evidence={ECO:0000269|PubMed:31439793};
CC -!- DOMAIN: The TIR domain catalyzes the NAD(+) cleavage (NADase) activity
CC (PubMed:31439793). In contrast to classical TIR-NB-LRR receptor-like
CC proteins, only contains a TIR domain (Probable).
CC {ECO:0000269|PubMed:31439793, ECO:0000305}.
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DR EMBL; CM000880; KQK15683.1; -; Genomic_DNA.
DR RefSeq; XP_003560074.3; XM_003560026.3.
DR AlphaFoldDB; I1GTC2; -.
DR SMR; I1GTC2; -.
DR STRING; 15368.BRADI1G24377.1; -.
DR EnsemblPlants; KQK15683; KQK15683; BRADI_1g24377v3.
DR GeneID; 100831488; -.
DR Gramene; KQK15683; KQK15683; BRADI_1g24377v3.
DR KEGG; bdi:100831488; -.
DR eggNOG; ENOG502RXQV; Eukaryota.
DR HOGENOM; CLU_087415_1_0_1; -.
DR InParanoid; I1GTC2; -.
DR OMA; YFDSDFC; -.
DR OrthoDB; 1174835at2759; -.
DR Proteomes; UP000008810; Chromosome 1.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IDA:UniProtKB.
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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0019677; P:NAD catabolic process; IDA:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; 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 Hydrolase; NAD; Plant defense; Reference proteome.
FT CHAIN 1..224
FT /note="TIR-only protein"
FT /id="PRO_0000448796"
FT DOMAIN 51..178
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 60..65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:V9M398"
FT BINDING 93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:V9M398"
SQ SEQUENCE 224 AA; 25017 MW; 2E9B7180D65B3DD1 CRC64;
MASSGLSSRR SIMASRLTAS AEAVNEPRRG AVVSRRVEYD EESLAGAGGE SRYEVFINHR
GVDTKRTVAR LLYDRLAQAG LRGFLDNMSM RPGDRLEERI GSAIRECTVA VAIFSPSYCD
SEYCLRELAM LVESRKAIIP IFYDIKPSDL LLPQAVADSE VYLPRDLERF KFALREAKHT
VGITYDSATG DMAELVSAAA DAVMYNMEKM ETVQRRETMI LSRL
