ID B6H451_PENRW Unreviewed; 525 AA. AC B6H451; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 06-JUL-2016, entry version 62. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928}; DE Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156}; DE Short=IMPD {ECO:0000256|HAMAP-Rule:MF_03156}; DE Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_03156}; DE EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928}; GN ORFNames=Pc13g07630 {ECO:0000313|EMBL:CAP91832.1}, PCH_Pc13g07630 GN {ECO:0000313|EMBL:CAP91832.1}; OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / OS Wisconsin 54-1255) (Penicillium chrysogenum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium; OC Penicillium chrysogenum complex. OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP91832.1, ECO:0000313|Proteomes:UP000000724}; RN [1] {ECO:0000313|EMBL:CAP91832.1, ECO:0000313|Proteomes:UP000000724} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255 RC {ECO:0000313|Proteomes:UP000000724}; RX PubMed=18820685; DOI=10.1038/nbt.1498; RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M., RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M., RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F., RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., RA van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H., RA Wagner C., Wortman J.R., Bovenberg R.A.L.; RT "Genome sequencing and analysis of the filamentous fungus Penicillium RT chrysogenum."; RL Nat. Biotechnol. 26:1161-1168(2008). CC -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) CC to xanthosine 5'-phosphate (XMP), the first committed and rate- CC limiting step in the de novo synthesis of guanine nucleotides, and CC therefore plays an important role in the regulation of cell CC growth. {ECO:0000256|HAMAP-Rule:MF_03156}. CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O = CC xanthosine 5'-phosphate + NADH. {ECO:0000256|HAMAP-Rule:MF_03156, CC ECO:0000256|RuleBase:RU003928}. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03156}; CC -!- ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive CC inhibitor that prevents formation of the closed enzyme CC conformation by binding to the same site as the amobile flap. In CC contrast, mizoribine monophosphate (MZP) is a competitive CC inhibitor that induces the closed conformation. MPA is a potent CC inhibitor of mammalian IMPDHs but a poor inhibitor of the CC bacterial enzymes. MZP is a more potent inhibitor of bacterial CC IMPDH. {ECO:0000256|HAMAP-Rule:MF_03156}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; CC XMP from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_03156, CC ECO:0000256|RuleBase:RU003928}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03156}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000256|HAMAP- CC Rule:MF_03156, ECO:0000256|RuleBase:RU003927}. CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000256|HAMAP- CC Rule:MF_03156}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM920428; CAP91832.1; -; Genomic_DNA. DR RefSeq; XP_002559192.1; XM_002559146.1. DR ProteinModelPortal; B6H451; -. DR STRING; 500485.XP_002559192.1; -. DR EnsemblFungi; CAP91832; CAP91832; PCH_Pc13g07630. DR GeneID; 8309924; -. DR KEGG; pcs:Pc13g07630; -. DR eggNOG; KOG2550; Eukaryota. DR eggNOG; COG0516; LUCA. DR eggNOG; COG0517; LUCA. DR HOGENOM; HOG000165752; -. DR KO; K00088; -. DR OMA; KQITMKT; -. DR OrthoDB; EOG793BHK; -. DR BioCyc; PCHR:PC13G07630-MONOMER; -. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000000724; Contig Pc00c13. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01964; IMPDH; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR005990; IMP_DH. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR PANTHER; PTHR11911:SF6; PTHR11911:SF6; 2. DR Pfam; PF00571; CBS; 2. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000130; IMPDH; 1. DR SMART; SM00116; CBS; 2. DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 3: Inferred from homology; KW CBS domain {ECO:0000256|HAMAP-Rule:MF_03156}; KW Complete proteome {ECO:0000313|Proteomes:UP000000724}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}; KW GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_03156, KW ECO:0000256|RuleBase:RU003928}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03156, KW ECO:0000256|RuleBase:RU003928}; KW NAD {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|PIRSR:PIRSR000130-3, KW ECO:0000256|RuleBase:RU003928}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03156, KW ECO:0000256|RuleBase:RU003927}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_03156, KW ECO:0000256|PIRSR:PIRSR000130-4, ECO:0000256|RuleBase:RU003928}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03156, KW ECO:0000256|RuleBase:RU003928}; KW Reference proteome {ECO:0000313|Proteomes:UP000000724}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_03156}. FT DOMAIN 120 179 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 183 239 CBS. {ECO:0000259|PROSITE:PS51371}. FT NP_BIND 276 278 NAD. {ECO:0000256|HAMAP-Rule:MF_03156, FT ECO:0000256|PIRSR:PIRSR000130-3}. FT NP_BIND 326 328 NAD. {ECO:0000256|HAMAP-Rule:MF_03156, FT ECO:0000256|PIRSR:PIRSR000130-3}. FT REGION 366 368 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_03156}. FT REGION 389 390 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_03156}. FT ACT_SITE 333 333 Thioimidate intermediate. FT {ECO:0000256|HAMAP-Rule:MF_03156, FT ECO:0000256|PIRSR:PIRSR000130-1}. FT ACT_SITE 439 439 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_03156, ECO:0000256|PIRSR:PIRSR000130- FT 1}. FT METAL 328 328 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_03156, FT ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 330 330 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_03156, FT ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 333 333 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_03156, FT ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 506 506 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000256|HAMAP-Rule:MF_03156}. FT BINDING 331 331 IMP. {ECO:0000256|HAMAP-Rule:MF_03156}. FT BINDING 451 451 IMP. {ECO:0000256|HAMAP-Rule:MF_03156}. SQ SEQUENCE 525 AA; 55770 MW; 32FB96F633F21DED CRC64; MVEVLDYTKA LEVLKEYPGD GLHVDTLLDS DSHGALTYND FLILPGSITF PASDVSLETK VTRRFTIKAP LLSSPMDTVT EHSMAIHMAL LGGLGVIHNN CPPDEQAEMV RKVKRYENGF IQDPIVLSPE TTVGEAKELK TKWGFGGFPV TEKGTLLSKL LGIVTSRDIQ FHKNHEDPVT AVMMTDLVTA PAGTTLAEAN EVLRSSKKGK LPIVDKDGSL ISLLSRSDLM KNIHYPLASK LPSKQLLCAA AISTHDADKV RLEKLVDAGL DIVVVDSSQG HSIFQIAMIK YIKQTFPDID VIGGNIVTRE QAAALIAAGA DGLRIGMGSG SACITQEVMA AGRPQAAAVR SVSAFAARFG VPTIADGGVQ NLGHIVKGLA LGASAVMMGS LLAGTTESPG EYFMSSEGQL VKAFRGMGSI AVMEDKSKSG AGNNAGASRY FSENDKVKVA QGVAGSVIDR GSITQYVPYL VAGVQHSLQD IGVQNLDALR DGVNNGTVRF EMRSASAQTE GNVHGLHTHE KKLYS //