APTIR_ACTS5
ID APTIR_ACTS5 Reviewed; 720 AA.
AC G8SD34;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=NAD(+) hydrolase ApTIR {ECO:0000305};
DE EC=3.2.2.6 {ECO:0000269|PubMed:29395922};
DE AltName: Full=TIR domain-containing protein in actinoplanes {ECO:0000303|PubMed:29395922};
DE Short=ApTIR {ECO:0000303|PubMed:29395922};
GN OrderedLocusNames=ACPL_3149 {ECO:0000312|EMBL:AEV84044.1};
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Actinoplanes; unclassified Actinoplanes.
OX NCBI_TaxID=134676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110;
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) 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.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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; CP003170; AEV84044.1; -; Genomic_DNA.
DR RefSeq; WP_014690116.1; NC_017803.1.
DR AlphaFoldDB; G8SD34; -.
DR SMR; G8SD34; -.
DR STRING; 134676.ACPL_3149; -.
DR EnsemblBacteria; AEV84044; AEV84044; ACPL_3149.
DR KEGG; ase:ACPL_3149; -.
DR PATRIC; fig|134676.3.peg.3069; -.
DR eggNOG; COG2319; Bacteria.
DR HOGENOM; CLU_383876_0_0_11; -.
DR OMA; KIWLDET; -.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 2.130.10.10; -; 3.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015032; MTH538_TIR-like_domain.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08937; DUF1863; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00255; TIR; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50104; TIR; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Hydrolase; Membrane; NAD; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; WD repeat.
FT CHAIN 1..720
FT /note="NAD(+) hydrolase ApTIR"
FT /id="PRO_0000449139"
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..131
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REPEAT 420..459
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 465..504
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 510..549
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 555..594
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 600..639
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 645..684
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 690..720
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 231..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 313..362
FT /evidence="ECO:0000255"
FT ACT_SITE 84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 10..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
SQ SEQUENCE 720 AA; 77624 MW; C69CFD98489FB00D CRC64;
MRYDAFISYS HAADGALAPA VQRGLQRLAR RWHRPRALEV FRDQTGLAVS HALWSSIKVA
LDQSEFFVLL ASPEAAASPW VNQEIEHWLS RHSVDRLLPV VTSGEWVWDA DAGDVDLERS
TAVPPALRGV FGEEPRHLDL RWARAEHELD LRHGRFRDAI AELAAGMHGM SKEDLDGEDV
IRHRQMLRMR RGALAVVCAL LLLVAGTAVA WRNARGEVTA TNVALQRQRA ATAAEQHRTE
EAADQARSQQ QIVEAEQQRA QKAAEEARGQ QAVAEAEQQR ALRAAGEARR QEGIAAAEQR
RAQKAAAEAR RQRGVADAEK AKANRAAAEA ERQRKIAADE QRKAHEAAAE AERQREEAVK
QQRIAIGRRL LGQAGEARDR DPRTAIQLGI AARHIYPGPQ SQAGLVETLV RTHYAGTVTG
HTAVVSAVAL SGDGRTLVTD GLDGTVMVWD PTDRAAPRRL AQLTSSTAPV YTVALSGDGR
TLVTGSEDGT AMVWDLTDRA APRRLAQLTG HTDVVDAVAL SGDGRTLATG SFDGTAMVWD
VTDRAAPRRL AQLTDHTAPV TAVALSGDGR TLATGSDDHT AMVWDLTDRA APRRLAQLTG
HTAGVDAVAL SGDGRTLATG SYDGTAMLWD LTDRAAPRRL AQLTGHTAQV YTVALSRDGR
TLATGSEDHT AMVWDLTDRA APRRLAQLTG HTDAVDAVAL SGDGRTLATA ASITRRCCGM
