ID   B6H451_PENCW            Unreviewed;       525 AA.
AC   B6H451;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   30-NOV-2010, entry version 17.
DE   RecName: Full=Inosine-5'-monophosphate dehydrogenase;
DE            EC=1.1.1.205;
GN   ORFNames=Pc13g07630;
OS   Penicillium chrysogenum (strain ATCC 28089 / DSM 1075 / Wisconsin
OS   54-1255) (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Penicillium;
OC   Penicillium chrysogenum complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
CC       XMP from IMP: step 1/1.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
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DR   EMBL; AM920428; CAP91832.1; -; Genomic_DNA.
DR   RefSeq; XP_002559192.1; XM_002559146.1.
DR   ProteinModelPortal; B6H451; -.
DR   GeneID; 8309924; -.
DR   KEGG; pcs:Pc13g07630; -.
DR   OrthoDB; EOG92Z66Q; -.
DR   BioCyc; PCHR:PC13G07630-MONOMER; -.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   InterPro; IPR005990; IMP_DH.
DR   InterPro; IPR018529; IMP_DH-rel.
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; 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; GMP biosynthesis; Metal-binding; NAD;
KW   Oxidoreductase; Potassium; Purine biosynthesis.
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
//