ID A0A1T1HEA0_OCELI Unreviewed; 481 AA.
AC A0A1T1HEA0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=NAD(+) hydrolase ThsA {ECO:0000256|ARBA:ARBA00035033};
DE EC=3.2.2.5 {ECO:0000256|ARBA:ARBA00034327};
GN ORFNames=BTA35_0201245 {ECO:0000313|EMBL:OOV88191.1};
OS Oceanospirillum linum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Oceanospirillum.
OX NCBI_TaxID=966 {ECO:0000313|EMBL:OOV88191.1, ECO:0000313|Proteomes:UP000190064};
RN [1] {ECO:0000313|EMBL:OOV88191.1, ECO:0000313|Proteomes:UP000190064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11336 {ECO:0000313|EMBL:OOV88191.1,
RC ECO:0000313|Proteomes:UP000190064};
RA Trachtenberg A.M., Carney J.G., Linnane J.D., Rheaume B.A., Pitts N.L.,
RA Mykles D.L., Maclea K.S.;
RT "Draft Genome Sequence of the Salt Water Bacterium Oceanospirillum linum
RT ATCC 11336.";
RL Submitted (FEB-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOV88191.1}.
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DR EMBL; MTSD02000001; OOV88191.1; -; Genomic_DNA.
DR RefSeq; WP_077242608.1; NZ_MTSD02000001.1.
DR AlphaFoldDB; A0A1T1HEA0; -.
DR STRING; 966.BTA35_0201245; -.
DR Proteomes; UP000190064; 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:UP000190064}.
FT DOMAIN 6..300
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
SQ SEQUENCE 481 AA; 54560 MW; 26F18275527EACA6 CRC64;
MKVTTDQQRQ RFVQELLKDL TEENLAIFAG AGLSAPAGFV SWSELLRPVA EELELEIEKE
TDLVALAQYH CNSNLANRGK LNQLLINELS DNAKITENHQ ILARLPISTY WTTNYDKLIE
NSLKETGKIP DTKYRIKQLS FTKRGRDAVV YKMHGDIEHP DEAVLTKDDY ETYHVKMQPF
INALSGDLVA KTFLFLGFSF TDPNLDYILS RVRVAYSTDQ RQHYCIQKLV EPKDGEPEAD
TEYRARKQEL FIQDLLRFGI KTILVSSYAE ITDILQQIEW AFKRNTIFIS GSAHEYGRWE
PSVAENFIYS LAKEISSLGF RIVSGFGLGV GSSVITGALE HVYMSGLRLD SDQLILRPFP
QTEVGTRPIA QVWHDYRTDM ISYSGIAIFL FGNKLKDGEV VVADGLIKEF EIAKSNGLLL
IPVGATEYAS RQIYCQLLKE GYFDSDAFPE NARKFINQIC DKESELTTIQ SGVIDLLKSL
K
//
