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Database: UniProt
Entry: A0A1I4K4D8_9BACI
LinkDB: A0A1I4K4D8_9BACI
Original site: A0A1I4K4D8_9BACI 
ID   A0A1I4K4D8_9BACI        Unreviewed;       481 AA.
AC   A0A1I4K4D8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=NAD(+) hydrolase ThsA {ECO:0000256|ARBA:ARBA00035033};
DE            EC=3.2.2.5 {ECO:0000256|ARBA:ARBA00034327};
GN   ORFNames=SAMN04487943_103350 {ECO:0000313|EMBL:SFL73660.1};
OS   Gracilibacillus orientalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX   NCBI_TaxID=334253 {ECO:0000313|EMBL:SFL73660.1, ECO:0000313|Proteomes:UP000198565};
RN   [1] {ECO:0000313|EMBL:SFL73660.1, ECO:0000313|Proteomes:UP000198565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.4250 {ECO:0000313|EMBL:SFL73660.1,
RC   ECO:0000313|Proteomes:UP000198565};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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=3.2.2.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00034990};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC         Evidence={ECO:0000256|ARBA:ARBA00034990};
CC   -!- SIMILARITY: Belongs to the soluble Thoeris ThsA family.
CC       {ECO:0000256|ARBA:ARBA00035014}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00236}.
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DR   EMBL; FOTR01000003; SFL73660.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4K4D8; -.
DR   STRING; 334253.SAMN04487943_103350; -.
DR   OrthoDB; 1688888at2; -.
DR   Proteomes; UP000198565; Unassembled WGS sequence.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   CDD; cd01406; SIR2-like; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR039444; SIR2-like.
DR   InterPro; IPR026590; Ssirtuin_cat_dom.
DR   InterPro; IPR041486; ThsA_STALD.
DR   Pfam; PF13289; SIR2_2; 1.
DR   Pfam; PF18185; STALD; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          1..283
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
SQ   SEQUENCE   481 AA;  54304 MW;  A0B2D00E1CBC07AE CRC64;
     MEYNPSIQEF LRTYVKAIQD SNAAIFAGAG LSRPAGYVDW KELLREVAQD LQLDIDQESD
     LIALAQYHVN EFSGRGKINQ ILIEEFTRSV STSHNHKILS HLPISTYWTT NYDQLIETNL
     EAVGKKVDKK ITSETMTYSV PGSDVTVYKM HGDSTLPHDA VLTKDDYEGY DQKRQIYSTA
     LRGDLVSKTF LFIGFSFDDP NLSQILSRIR ILLNENKRTH YCFMKKVKAN DFNGNDDEFR
     YAEIKQNLKI KDLMRYGIKV LLIDDYPEIT EILQHIASLI IRKNIFVSGS ASDYGDWGEE
     KSFEFSTSLS KALIKNNNNI VSGFGLGIGS CIISGALEEL YSSQNNKVEQ RLKCRPFPQN
     TTGGLSIKDL WTKYRNDMIS NIGISVFIFG NKIDTETKDV IDANGMVEEF DISIEKGAIP
     IPVGATGFTS KILWQRVMDD FGPLVGIEDL KPLYSDLGDE SKNSEELIET VVKIINLLAK
     H
//
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