ID   A0A4T1ZUW9_9PSED        Unreviewed;       275 AA.
AC   A0A4T1ZUW9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   26-FEB-2020, entry version 6.
DE   RecName: Full=NADH pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00297, ECO:0000256|SAAS:SAAS00345522};
DE            EC=3.6.1.22 {ECO:0000256|HAMAP-Rule:MF_00297, ECO:0000256|SAAS:SAAS00042483};
GN   Name=nudC {ECO:0000256|HAMAP-Rule:MF_00297};
GN   ORFNames=D8779_11205 {ECO:0000313|EMBL:TIH08085.1};
OS   Pseudomonas leptonychotis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2448482 {ECO:0000313|EMBL:TIH08085.1, ECO:0000313|Proteomes:UP000307541};
RN   [1] {ECO:0000313|EMBL:TIH08085.1, ECO:0000313|Proteomes:UP000307541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 8849 {ECO:0000313|EMBL:TIH08085.1,
RC   ECO:0000313|Proteomes:UP000307541};
RA   Novakova D., Svec P., Kralova S., Kristofova L., Zeman M., Pantucek R.,
RA   Maslanova I., Sedlacek I.;
RT   "Pseudomonas leptonychotis sp. nov., isolated from Weddell seals in
RT   Antarctica.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2
CC         H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215;
CC         EC=3.6.1.22; Evidence={ECO:0000256|HAMAP-Rule:MF_00297,
CC         ECO:0000256|SAAS:SAAS01118353};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-
CC         ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832,
CC         ChEBI:CHEBI:456215; EC=3.6.1.22; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00297, ECO:0000256|SAAS:SAAS01118352};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00608010};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00297,
CC       ECO:0000256|SAAS:SAAS00042551}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00297, ECO:0000256|SAAS:SAAS00541212}.
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:TIH08085.1}.
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DR   EMBL; RFLV01000002; TIH08085.1; -; Genomic_DNA.
DR   Proteomes; UP000307541; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00297; Nudix_NudC; 1.
DR   InterPro; IPR015375; NADH_PPase-like_N.
DR   InterPro; IPR022925; NADH_pyroPase_NudC.
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   Pfam; PF00293; NUDIX; 1.
DR   Pfam; PF09296; NUDIX-like; 1.
DR   Pfam; PF09297; zf-NADH-PPase; 1.
DR   SUPFAM; SSF55811; SSF55811; 2.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00297, ECO:0000256|SAAS:SAAS00437314,
KW   ECO:0000313|EMBL:TIH08085.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00297, ECO:0000256|SAAS:SAAS00016165};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00297, ECO:0000256|SAAS:SAAS00016184};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00297,
KW   ECO:0000256|SAAS:SAAS00016198};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00297, ECO:0000256|SAAS:SAAS00016191};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00297, ECO:0000256|SAAS:SAAS01085471}.
FT   DOMAIN          138..261
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
FT   MOTIF           172..193
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00297"
FT   METAL           111
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00297"
FT   METAL           114
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00297"
FT   METAL           129
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00297"
FT   METAL           132
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00297"
FT   METAL           187
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00297"
FT   METAL           191
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00297"
SQ   SEQUENCE   275 AA;  31015 MW;  5051099A42DB561B CRC64;
     MQRWQPTLLD SQLPGGWVVA HFKQHFLADS NGVLFPREWL KQQDLPIVAE HGLGHFDGDA
     IYLLELSQPF DMQGCAWQSL RQFMLQGDAD TFKLLSYATQ IGTWASQHRF CGSCGETMQH
     IPGERAMHCV RCELQHYPRL SPSMIVLVTR GDEVLLARSP RFVSGVYSTL AGFVEAGESV
     EHCVAREVRE EVGVEIKNLQ YLGSQGWPFP HSLMLGFHAE YDSGDIVMQA DEIEDAQWFN
     VHDLPPLPAT RSIARHLIDV YVARRLGHPE PVLPG
//