ID NUDC_PSE14 Reviewed; 278 AA. AC Q48IH8; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=NADH pyrophosphatase; DE EC=3.6.1.22; GN Name=nudC; OrderedLocusNames=PSPPH_2609; OS Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=264730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005; RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., RA Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., RA Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., RA Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., RA Mansfield J.W., Collmer A., Buell R.; RT "Whole-genome sequence analysis of Pseudomonas syringae pv. RT phaseolicola 1448A reveals divergence among pathovars in genes RT involved in virulence and transposition."; RL J. Bacteriol. 187:6488-6498(2005). CC -!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = AMP + NMN. CC -!- COFACTOR: Divalent ions. Manganese or magnesium (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000058; AAZ35769.1; -; Genomic_DNA. DR RefSeq; YP_274803.1; -. DR GeneID; 3558368; -. DR GenomeReviews; CP000058_GR; PSPPH_2609. DR KEGG; psp:PSPPH_2609; -. DR NMPDR; fig|264730.3.peg.2595; -. DR HOGENOM; Q48IH8; -. DR OMA; Q48IH8; TWAREHR. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP. DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:HAMAP. DR HAMAP; MF_00297; -; 1. DR InterPro; IPR015375; NADH_PPase-like_N. DR InterPro; IPR000086; NUDIX_hydrolase_core. DR InterPro; IPR015376; Znr_NADH_PPase. DR Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF09296; NUDIX-like; 1. DR Pfam; PF09297; zf-NADH-PPase; 1. DR PROSITE; PS00893; NUDIX; FALSE_NEG. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Manganese; NAD. FT CHAIN 1 278 NADH pyrophosphatase. FT /FTId=PRO_0000232118. FT MOTIF 175 196 Nudix box. SQ SEQUENCE 278 AA; 31068 MW; 5D2D23DE5202D67F CRC64; MAHPERWTTA VLDVEADGGL AVVQSDQGFL LDTNGAMFPR GWLAGLDLPV QSEHGIGYFE GEPVYLLVLE RSVAVEGCSW QGLRQFMLEG DFAVFQMLGY AAQVSTWARE HRFCGACGRA TVQIRGERAM FCEHDNLRLY PRISPSMIVL VTRGDEILLA RSPRFVTGMY SALAGFVEPG ESAEDCVHRE VMEEVQVRIK NLKYMGSQCW PFPHSMMLGF HAEYDSGDIV PQAEEIEDAR WFHIDDLPPL PANRSIARYL IEAYLAERSG APEPVLPG //