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Database: UniProt
Entry: S3K2H0_TREMA
LinkDB: S3K2H0_TREMA
Original site: S3K2H0_TREMA 
ID   S3K2H0_TREMA            Unreviewed;       265 AA.
AC   S3K2H0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE            EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN   ORFNames=HMPREF9194_00431 {ECO:0000313|EMBL:EPF32433.1};
OS   Treponema maltophilum ATCC 51939.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=1125699 {ECO:0000313|EMBL:EPF32433.1, ECO:0000313|Proteomes:UP000014541};
RN   [1] {ECO:0000313|EMBL:EPF32433.1, ECO:0000313|Proteomes:UP000014541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51939 {ECO:0000313|EMBL:EPF32433.1,
RC   ECO:0000313|Proteomes:UP000014541};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Leonetti C., Blanton J.M.,
RA   Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Treponema maltophilum ATCC 51939.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC         end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-
CC         nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876,
CC         Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029,
CC         ChEBI:CHEBI:144051; Evidence={ECO:0000256|ARBA:ARBA00023679};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877;
CC         Evidence={ECO:0000256|ARBA:ARBA00023679};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC       {ECO:0000256|ARBA:ARBA00009595}.
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:EPF32433.1}.
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DR   EMBL; ATFF01000002; EPF32433.1; -; Genomic_DNA.
DR   RefSeq; WP_016524730.1; NZ_KE332518.1.
DR   AlphaFoldDB; S3K2H0; -.
DR   STRING; 1125699.HMPREF9194_00431; -.
DR   PATRIC; fig|1125699.3.peg.437; -.
DR   eggNOG; COG2816; Bacteria.
DR   HOGENOM; CLU_037162_0_1_12; -.
DR   OrthoDB; 9787476at2; -.
DR   Proteomes; UP000014541; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd03429; NADH_pyrophosphatase; 1.
DR   Gene3D; 3.90.79.20; -; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR049734; NudC-like_C.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR015376; Znr_NADH_PPase.
DR   PANTHER; PTHR42904:SF6; NAD-CAPPED RNA HYDROLASE NUDT12; 1.
DR   PANTHER; PTHR42904; NUDIX HYDROLASE, NUDC SUBFAMILY; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   Pfam; PF09297; zf-NADH-PPase; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014541}.
FT   DOMAIN          133..259
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   265 AA;  30037 MW;  589D5C8A0294F621 CRC64;
     MPLISNPAEA AGGKVFLFSD NKLLVYADNV AVLPDTEVLK HFLRHHCISD WLYDSDYDYT
     AARLEKDSPV SDRFCWLPLR SVFAAEYDFA FSASRATALL NWKAKTRFCS YCGNAMKDAE
     DETARVCVQC AHRVYPSLSP AIIVQVCKGD KLLLAKHSRR NTDIYTCLAG YVEAGENLED
     CVRREVFEET GIELAELRYV ASQSWPFPDQ LMAGFRAEWK SGDIQIQKNE ISDARWFDKN
     NLPEIPKPGS LAYKLITGVL DESRR
//
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