ID   A0A1M6KWQ8_MALRU        Unreviewed;       479 AA.
AC   A0A1M6KWQ8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=NAD(+) hydrolase ThsA {ECO:0000256|ARBA:ARBA00035033};
DE            EC=3.2.2.5 {ECO:0000256|ARBA:ARBA00034327};
GN   ORFNames=SAMN02745165_02825 {ECO:0000313|EMBL:SHJ63395.1};
OS   Malonomonas rubra DSM 5091.
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC   Geopsychrobacteraceae; Malonomonas.
OX   NCBI_TaxID=1122189 {ECO:0000313|EMBL:SHJ63395.1, ECO:0000313|Proteomes:UP000184171};
RN   [1] {ECO:0000313|EMBL:SHJ63395.1, ECO:0000313|Proteomes:UP000184171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5091 {ECO:0000313|EMBL:SHJ63395.1,
RC   ECO:0000313|Proteomes:UP000184171};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQZT01000011; SHJ63395.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6KWQ8; -.
DR   STRING; 1122189.SAMN02745165_02825; -.
DR   OrthoDB; 5480778at2; -.
DR   Proteomes; UP000184171; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184171}.
FT   DOMAIN          1..262
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
SQ   SEQUENCE   479 AA;  54391 MW;  35DD14B9AD116E4B CRC64;
     MNSEIELFIK EYLKEIEEDN AAIFAGTGLS VPAGAVDWKS LLKPLADELG LDIDKEYDLV
     TLAQFHCNEN GGNRSKINQL LLEELSVGDH PTDNHKILAR LPICTYWTTN YDKLIETALR
     SEGKVPDVKY TVPQLATTKP KRDAVIYKMH GDIDHPDTAV ITKDDYEKYS NNFGAYINAL
     SGDLVSKTFL FLGFSFTDPN LDYILSRVRI TFRENQRRHY CIFRKRSQLE GESDEDFKQA
     EIRQRLVIED LKRFNIKTIL IDDFQQITDI LSYIEGLYKR RKIFISGSAD VYDPWGQQAT
     EEFLFHLCSA LIEQDYKMVT GVGRGIGYAV VSGAINGTRT INCRIDDRVS MRPFPLVLPY
     GSDIGAVWED YRQDMIPRAG IALFLLGNKY QDGNLVLANG VRREFEIARE HGLVVVPIGA
     SGYMAKELWT EVDSDFDTFY PNPPDGFREA FSVLGVEVSH PNELIQIILD LVHVLTKEG
//