ID   ABTIR_ACIB9             Reviewed;         269 AA.
AC   A0A009IHW8;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=NAD(+) hydrolase AbTIR {ECO:0000305};
DE            EC=3.2.2.6 {ECO:0000269|PubMed:29395922};
DE   AltName: Full=TIR domain-containing protein in A.baumannii {ECO:0000303|PubMed:29395922};
DE            Short=AbTIR {ECO:0000303|PubMed:29395922};
GN   ORFNames=J512_3302 {ECO:0000312|EMBL:EXB04249.1};
OS   Acinetobacter baumannii (strain 1295743).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=1310613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1295743;
RA   Harris A.D., Johnson K.J., George J., Shefchek K., Daugherty S.C.,
RA   Parankush S., Sadzewicz L., Tallon L., Sengamalay N., Hazen T.H.,
RA   Rasko D.A.;
RT   "Comparative genomics and transcriptomics to identify genetic mechanisms
RT   underlying the emergence of carbapenem resistant Acinetobacter baumannii
RT   (CRAb).";
RL   Submitted (FEB-2014) 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).
CC   -!- FUNCTION: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+)
CC       into ADP-D-ribose (ADPR) and nicotinamide (PubMed:29395922). In
CC       addition to ADPR, also generates a cyclization variant of cyclic ADPR
CC       (cADPR), termed v-cADPR, for which the cyclizing bond is unknown
CC       (PubMed:29395922). {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   -!- 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; JEWH01000055; EXB04249.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A009IHW8; -.
DR   SMR; A0A009IHW8; -.
DR   EnsemblBacteria; EXB04249; EXB04249; J512_3302.
DR   PATRIC; fig|1310613.3.peg.3172; -.
DR   Proteomes; UP000020595; Unassembled WGS sequence.
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   Coiled coil; Hydrolase; NAD.
FT   CHAIN           1..269
FT                   /note="NAD(+) hydrolase AbTIR"
FT                   /id="PRO_0000449138"
FT   DOMAIN          133..266
FT                   /note="TIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   COILED          31..99
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        208
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   BINDING         142..143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   BINDING         172
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
SQ   SEQUENCE   269 AA;  30922 MW;  4963BA0FB34B3ED7 CRC64;
     MSLEQKKGAD IISKILQIQN SIGKTTSPST LKTKLSEISR KEQENARIQS KLSDLQKKKI
     DIDNKLLKEK QNLIKEEILE RKKLEVLTKK QQKDEIEHQK KLKREIDAIK ASTQYITDVS
     ISSYNNTIPE TEPEYDLFIS HASEDKEDFV RPLAETLQQL GVNVWYDEFT LKVGDSLRQK
     IDSGLRNSKY GTVVLSTDFI KKDWTNYELD GLVAREMNGH KMILPIWHKI TKNDVLDYSP
     NLADKVALNT SVNSIEEIAH QLADVILNR