ID NUD12_MACFA Reviewed; 462 AA. AC Q4R7L8; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Peroxisomal NADH pyrophosphatase NUDT12; DE EC=3.6.1.22; DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 12; DE Short=Nudix motif 12; GN Name=NUDT12; ORFNames=QtsA-14876; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RG International consortium for macaque cDNA sequencing and analysis; RT "DNA sequences of macaque genes expressed in brain or testis and its RT evolutionary implications."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Hydrolyzes NAD(P)H to NMNH and AMP (2',5'-ADP), and CC diadenosine diphosphate to AMP. Has also activity towards CC NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to CC regulate the concentration of peroxisomal nicotinamide nucleotide CC cofactors required for oxidative metabolism in this organelle (By CC similarity). CC -!- CATALYTIC ACTIVITY: NAD(+) + H(2)O = AMP + NMN. CC -!- COFACTOR: Magnesium or manganese (By similarity). CC -!- SUBCELLULAR LOCATION: Peroxisome (By similarity). CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily. CC -!- SIMILARITY: Contains 3 ANK repeats. 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; AB168797; BAE00904.1; -; mRNA. DR HOVERGEN; Q4R7L8; -. DR BRENDA; 3.6.1.22; 3438. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:EC. DR InterPro; IPR002110; ANK. DR InterPro; IPR015375; NADH_PPase-like_N. DR InterPro; IPR000086; NUDIX_hydrolase_core. DR InterPro; IPR015376; Znr_NADH_PPase. DR Gene3D; G3DSA:1.25.40.20; ANK; 1. DR Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1. DR Pfam; PF00023; Ank; 2. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF09296; NUDIX-like; 1. DR Pfam; PF09297; zf-NADH-PPase; 1. DR SMART; SM00248; ANK; 3. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. DR PROSITE; PS00893; NUDIX; 1. PE 2: Evidence at transcript level; KW ANK repeat; Hydrolase; Magnesium; Manganese; Metal-binding; NAD; NADP; KW Peroxisome; Repeat. FT CHAIN 1 462 Peroxisomal NADH pyrophosphatase NUDT12. FT /FTId=PRO_0000260766. FT REPEAT 11 40 ANK 1. FT REPEAT 45 74 ANK 2. FT REPEAT 78 98 ANK 3. FT MOTIF 355 376 Nudix box. FT MOTIF 460 462 Microbody targeting signal (By FT similarity). FT METAL 370 370 Magnesium or manganese (By similarity). FT METAL 374 374 Magnesium or manganese (By similarity). SQ SEQUENCE 462 AA; 52092 MW; BD4B6171E80DCB25 CRC64; MSSVKRSPKQ EIVTQFHCSA AEGDIAKLTG ILSHSPSLLN ETSENGWTAL MYAARNGHPE IVQFLLEKGC DRSIVNKSRQ TALDIAVFWG YKHIANLLAT AKGGKKPWFL TNEVEECENY FSKTLLDRKS EKRNNADWLL AKESHPATVF ILFSDLNPLV TLGGNKESFQ QPEVRLCQLN YKDIKDYLAQ PEEITLIFLG VELEMKDKLL NYAGEVPREE EDGLVAWFAL GIDPIAAEEF KQRHENCYFL HPPMPALLQL KEKEAGVVAQ ARSVLAWHSR YKFCPTCGNG TKIEEGGYKR VCLKEDCPSL NGVHNTSYPR VDPVVIMQVI HPDGTRCLLG RQKRFPPGMF TCLAGFIEPG ETIEDAVRRE VEEESGVKVG HVQYVSCQPW PMPSSLMIGC LAVAVSTEIK VDKNEIEDAR WFTREQVLDV LTKGKQQAFF VPPSRAIAHQ LIKHWIRINP NL //