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Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205)

 A0A084G4N4_9PEZI        Unreviewed;       537 AA.
A0A084G4N4;
29-OCT-2014, integrated into UniProtKB/TrEMBL.
29-OCT-2014, sequence version 1.
27-SEP-2017, entry version 21.
RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928};
Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156};
Short=IMPD {ECO:0000256|HAMAP-Rule:MF_03156};
Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_03156};
EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928};
ORFNames=SAPIO_CDS6162 {ECO:0000313|EMBL:KEZ42296.1};
Scedosporium apiospermum.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae;
Scedosporium.
NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ42296.1, ECO:0000313|Proteomes:UP000028545};
[1] {ECO:0000313|EMBL:KEZ42296.1, ECO:0000313|Proteomes:UP000028545}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ42296.1,
ECO:0000313|Proteomes:UP000028545};
Vandeputte P., Rechenmann M., Bouchara J.-P.;
Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP)
to xanthosine 5'-phosphate (XMP), the first committed and rate-
limiting step in the de novo synthesis of guanine nucleotides, and
therefore plays an important role in the regulation of cell
growth. {ECO:0000256|HAMAP-Rule:MF_03156}.
-!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O =
xanthosine 5'-phosphate + NADH. {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003928}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|HAMAP-Rule:MF_03156};
-!- ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive
inhibitor that prevents formation of the closed enzyme
conformation by binding to the same site as the amobile flap. In
contrast, mizoribine monophosphate (MZP) is a competitive
inhibitor that induces the closed conformation. MPA is a potent
inhibitor of mammalian IMPDHs but a poor inhibitor of the
bacterial enzymes. MZP is a more potent inhibitor of bacterial
IMPDH. {ECO:0000256|HAMAP-Rule:MF_03156}.
-!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
XMP from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003928}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03156}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}.
-!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000256|HAMAP-
Rule:MF_03156, ECO:0000256|RuleBase:RU003927}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03156}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEZ42296.1}.
-----------------------------------------------------------------------
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EMBL; JOWA01000100; KEZ42296.1; -; Genomic_DNA.
RefSeq; XP_016642095.1; XM_016788338.1.
EnsemblFungi; KEZ42296; KEZ42296; SAPIO_CDS6162.
GeneID; 27725234; -.
UniPathway; UPA00601; UER00295.
Proteomes; UP000028545; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd00381; IMPDH; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_01964; IMPDH; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000644; CBS_dom.
InterPro; IPR005990; IMP_DH.
InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
InterPro; IPR001093; IMP_DH_GMPRt.
Pfam; PF00571; CBS; 2.
Pfam; PF00478; IMPDH; 1.
PIRSF; PIRSF000130; IMPDH; 1.
SMART; SM00116; CBS; 2.
TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
PROSITE; PS51371; CBS; 2.
PROSITE; PS00487; IMP_DH_GMP_RED; 1.
3: Inferred from homology;
CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
Complete proteome {ECO:0000313|Proteomes:UP000028545};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156};
GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003928};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003928};
NAD {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|PIRSR:PIRSR000130-3,
ECO:0000256|RuleBase:RU003928};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003927, ECO:0000313|EMBL:KEZ42296.1};
Potassium {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-4, ECO:0000256|RuleBase:RU003928};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003928};
Reference proteome {ECO:0000313|Proteomes:UP000028545}.
DOMAIN 127 186 CBS. {ECO:0000259|PROSITE:PS51371}.
DOMAIN 190 246 CBS. {ECO:0000259|PROSITE:PS51371}.
NP_BIND 284 286 NAD. {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-3}.
NP_BIND 334 336 NAD. {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-3}.
REGION 374 376 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_03156}.
REGION 397 398 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_03156}.
REGION 422 426 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_03156}.
ACT_SITE 341 341 Thioimidate intermediate.
{ECO:0000256|HAMAP-Rule:MF_03156}.
ACT_SITE 452 452 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_03156}.
METAL 336 336 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 338 338 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 341 341 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 519 519 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000256|HAMAP-Rule:MF_03156}.
BINDING 339 339 IMP. {ECO:0000256|HAMAP-Rule:MF_03156}.
BINDING 464 464 IMP. {ECO:0000256|HAMAP-Rule:MF_03156}.
SEQUENCE 537 AA; 57316 MW; 84D40CAC8B3E119B CRC64;
MSTLYGEGKV RDFKNAINDL SNYETRDGLD ITELMDTKKH GGLTYNDFLL LPGYIGFPAS
EVVLDSPVTK KISIKTPFVS SPMDTVTEHE MAIHMALQGG LGVIHHNCSA EAQADMVRKV
KRYENGFILD PVVIKRTTTV GEAFDLKLKW GFGGFPVTET GSVGSKLLGI VTNRDIQFET
DLDQPVENVM VTDLITAQAG ITLAEANQIL KDSKKGKLPI VDKDFNLVSM ISRSDLNKNQ
DFPLSSKAPD SKQLIAAAAI GTRPEDKVRL QKLVDAGLDI VVLDSSQGNS MYQIEMIKWI
KEKFPKLEVI GGNVVTREQA ASLIQAGVDG LRIGMGSGSA CITQEVMAVG RPQAAAVYSV
SSFAAQYGVP CIADGGVQNV GHIVKGLALG AATVMMGGLL AGTTESPGTS FVSREGKLVK
AYRGMGSIDA MQDKKAGNGG KDSQRSNAGT ARYFSEGDSV LVAQGVSGSV AHRGPIGKFV
PYLAAGLKHS MQDCGIQSLK ELHEGVAAGL VRFELRTSSA QAEGNVNMES YEKKLFA


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