ID B6H451_PENRW Unreviewed; 525 AA. AC B6H451; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 16-MAR-2016, entry version 60. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|RuleBase:RU003928}; DE EC=1.1.1.205 {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 -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O = CC xanthosine 5'-phosphate + NADH. {ECO:0000256|RuleBase:RU003928}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; CC XMP from IMP: step 1/1. {ECO:0000256|RuleBase:RU003928}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC {ECO:0000256|RuleBase:RU003927}. 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:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW. 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 Complete proteome {ECO:0000313|Proteomes:UP000000724}; KW GMP biosynthesis {ECO:0000256|RuleBase:RU003928}; KW Metal-binding {ECO:0000256|RuleBase:RU003928}; KW NAD {ECO:0000256|PIRSR:PIRSR000130-3, ECO:0000256|RuleBase:RU003928}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003927}; KW Potassium {ECO:0000256|PIRSR:PIRSR000130-4, KW ECO:0000256|RuleBase:RU003928}; KW Purine biosynthesis {ECO:0000256|RuleBase:RU003928}; KW Reference proteome {ECO:0000313|Proteomes:UP000000724}. 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|PIRSR:PIRSR000130-3}. FT NP_BIND 326 328 NAD. {ECO:0000256|PIRSR:PIRSR000130-3}. FT ACT_SITE 333 333 Thioimidate intermediate. FT {ECO:0000256|PIRSR:PIRSR000130-1}. FT ACT_SITE 439 439 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000130-1}. FT METAL 328 328 Potassium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 330 330 Potassium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 333 333 Potassium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000130-4}. 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 //