ID   B6H451_PENCW            Unreviewed;       525 AA.
AC   B6H451;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   11-DEC-2013, entry version 41.
DE   SubName: Full=Pc13g07630 protein;
GN   ORFNames=Pc13g07630, PCH_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; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / Wisconsin 54-1255;
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.
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DR   EMBL; AM920428; CAP91832.1; -; Genomic_DNA.
DR   RefSeq; XP_002559192.1; XM_002559146.1.
DR   ProteinModelPortal; B6H451; -.
DR   STRING; 500485.B6H451; -.
DR   GeneID; 8309924; -.
DR   KEGG; pcs:Pc13g07630; -.
DR   eggNOG; COG0517; -.
DR   HOGENOM; HOG000165752; -.
DR   KO; K00088; -.
DR   OMA; TEGAMAI; -.
DR   OrthoDB; EOG793BHK; -.
DR   BioCyc; PCHR:PC13G07630-MONOMER; -.
DR   UniPathway; UPA00601; UER00295.
DR   GO; GO:0030554; F:adenyl nucleotide binding; IEA:InterPro.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
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; 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.
FT   ACT_SITE    333    333       Thioimidate intermediate (By similarity).
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
//