ID   B6H451_PENRW            Unreviewed;       525 AA.
AC   B6H451;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   03-MAY-2023, entry version 94.
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 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species 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., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   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) to
CC       xanthosine 5'-phosphate (XMP), the first committed and rate-limiting
CC       step in the de novo synthesis of guanine nucleotides, and therefore
CC       plays an important role in the regulation of cell growth.
CC       {ECO:0000256|HAMAP-Rule:MF_03156}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053;
CC         EC=1.1.1.205; Evidence={ECO:0000256|HAMAP-Rule:MF_03156,
CC         ECO:0000256|RuleBase:RU003928};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03156};
CC   -!- ACTIVITY REGULATION: Mycophenolic acid (MPA) is a non-competitive
CC       inhibitor that prevents formation of the closed enzyme conformation by
CC       binding to the same site as the amobile flap. In contrast, mizoribine
CC       monophosphate (MZP) is a competitive inhibitor that induces the closed
CC       conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor
CC       inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of
CC       bacterial IMPDH. {ECO:0000256|HAMAP-Rule:MF_03156}.
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC       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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03156}.
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DR   EMBL; AM920428; CAP91832.1; -; Genomic_DNA.
DR   RefSeq; XP_002559192.1; XM_002559146.1.
DR   AlphaFoldDB; B6H451; -.
DR   STRING; 1108849.XP_002559192.1; -.
DR   GeneID; 8309924; -.
DR   KEGG; pcs:Pc13g07630; -.
DR   VEuPathDB; FungiDB:PCH_Pc13g07630; -.
DR   eggNOG; KOG2550; Eukaryota.
DR   HOGENOM; CLU_022552_2_1_1; -.
DR   OMA; NCPPDEQ; -.
DR   OrthoDB; 166969at2759; -.
DR   BioCyc; PCHR:PC13G07630-MON; -.
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-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04601; CBS_pair_IMPDH; 1.
DR   CDD; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01964; IMPDH; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005990; IMP_DH.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000130; IMPDH; 1.
DR   SMART; SM00116; CBS; 2.
DR   SMART; SM01240; IMPDH; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
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|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703}; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03156};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|PIRSR:PIRSR000130-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_03156};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_03156};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03156,
KW   ECO:0000256|RuleBase:RU003928};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT   DOMAIN          120..179
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          183..239
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   REGION          506..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        333
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-1"
FT   ACT_SITE        439
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-1"
FT   BINDING         276..278
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         326..328
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         328
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         330
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         331
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT   BINDING         333
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT                   ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         366..368
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT   BINDING         389..390
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT   BINDING         451
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT   BINDING         506
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /evidence="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
//