ID GMPR2_BOVIN Reviewed; 348 AA. AC Q32L93; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 16-JUN-2009, entry version 31. DE RecName: Full=GMP reductase 2; DE EC=1.7.1.7; DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase 2; DE Short=Guanosine monophosphate reductase 2; GN Name=GMPR2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Liver; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination CC of GMP to IMP. It functions in the conversion of nucleobase, CC nucleoside and nucleotide derivatives of G to A nucleotides, and CC in maintaining the intracellular balance of A and G nucleotides. CC Plays a role in modulating cellular differentiation (By CC similarity). CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NH(3) + NADP(+) = CC guanosine 5'-phosphate + NADPH. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. 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; BC109695; AAI09696.1; -; mRNA. DR IPI; IPI00706578; -. DR RefSeq; NP_001033208.1; -. DR UniGene; Bt.76123; -. DR SMR; Q32L93; 10-337. DR Ensembl; ENSBTAG00000002715; Bos taurus. DR GeneID; 515837; -. DR KEGG; bta:515837; -. DR HOVERGEN; Q32L93; -. DR BRENDA; 1.7.1.7; 251. DR GO; GO:0003920; F:GMP reductase activity; IEA:EC. DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005993; GMP_reduct1. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000235; GMP_reductase; 1. DR TIGRFAMs; TIGR01305; GMP_reduct_1; 1. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 2: Evidence at transcript level; KW Metal-binding; NADP; Oxidoreductase; Potassium. FT CHAIN 1 348 GMP reductase 2. FT /FTId=PRO_0000253472. FT NP_BIND 108 131 NADP (By similarity). FT ACT_SITE 186 186 Thioimidate intermediate (By similarity). FT METAL 181 181 Potassium; via carbonyl oxygen (By FT similarity). FT METAL 183 183 Potassium; via carbonyl oxygen (By FT similarity). FT BINDING 219 219 NADP (By similarity). SQ SEQUENCE 348 AA; 38033 MW; B4DA9AF8BC5474D2 CRC64; MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV DLTRSFAFRN SKQMYTGIPI IAANMDTVGT FEMAKVLCKF SLFTAVHKHY SLEQWKEFAS QNPDCLEHLA ASSGTGSSDF EQLEQILNAI PQVKYVCLDV ANGYSEHFVE FVKDVRKRFP EHTIMAGNVV TGEMVEELIL SGADIIKVGI GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM LGGMLAGHSE SGGELIERNG RKYKLFYGMS SEMAMKKYAG GVAEYRASEG KTVEVPFKGD VEHTIRDIIG GIRSTCTYVG AAKQKELSRR TTFIRVTQQV KPIFSDES //