ID A0A078HCA2_BRANA Unreviewed; 504 AA.
AC A0A078HCA2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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 Name=BnaA06g10940D {ECO:0000313|EMBL:CDY35084.1};
GN ORFNames=DARMORV10_A06P12260.1 {ECO:0000313|EMBL:CAF2083480.1},
GN GSBRNA2T00057955001 {ECO:0000313|EMBL:CDY35084.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY35084.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY35084.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
RN [2] {ECO:0000313|EMBL:CDY35084.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAF2083480.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope - CEA;
RA William W.;
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00024264,
CC ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958,
CC 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.
CC {ECO:0000256|ARBA:ARBA00005502, ECO:0000256|HAMAP-Rule:MF_03156,
CC 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; HG994360; CAF2083480.1; -; Genomic_DNA.
DR EMBL; LK032346; CDY35084.1; -; Genomic_DNA.
DR STRING; 3708.A0A078HCA2; -.
DR PaxDb; 3708-A0A078HCA2; -.
DR EnsemblPlants; CDY35084; CDY35084; GSBRNA2T00057955001.
DR Gramene; CDY35084; CDY35084; GSBRNA2T00057955001.
DR OMA; ISPSMTH; -.
DR UniPathway; UPA00601; UER00295.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IBA:GO_Central.
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 GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central.
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; IPR005990; IMP_DH.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR NCBIfam; TIGR01302; IMP_dehydrog; 1.
DR PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP-
KW Rule:MF_03156};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03156};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03156};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03156,
KW ECO:0000256|RuleBase:RU003927};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_03156};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_03156}; Reference proteome {ECO:0000313|Proteomes:UP000028999}.
FT DOMAIN 20..494
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 323
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT ECO:0000256|PIRSR:PIRSR000130-1"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156,
FT ECO:0000256|PIRSR:PIRSR000130-1"
FT BINDING 266..268
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 316..318
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 318
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 320
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 321
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT BINDING 323
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 356..358
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT BINDING 379..380
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT BINDING 403..407
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
FT BINDING 431
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156"
SQ SEQUENCE 504 AA; 54164 MW; 0134D3C6001F75B9 CRC64;
MASGFEDGFS AEKLFAQGYS YTYDDVIFLP HYIDFSTDAV SLSTRLSKRV PLSIPCVASP
MDTVSESHMA AAMAALGGIG IVHYNCDTAT QASLIRHAKS LRVPIASDAV FKCPDHLIGS
VDDFGPSSFV FVSQTVGTLT PSLLGYVSKS EWSSMKDEQK EMKIYDYMRS CESRDYYVPW
DIDLDKIDAV LEDKQKGFVV LEKDGETVNV VTKDDVERVK GYPKLGSGTV GPDGKWMVGA
AIGTRESDKE RLEHLVKAGA NVVVLDSSQG NSIYQIEMIK YVKNLYPELD VVGGNVVTMY
QAENLIKAGV DGLRVGMGSG SICTTQEVCA VGRGQATAVY KVSTLAAQHG VPVIADGGIS
NSGHIVKALV LGASTVMMGS FLAGSTEAPG AYEYRNGRRV KKYRGMGSLE AMTKGSDQRY
LGDTAKLKIA QGVVGAVADK GSVLKFIPYT MHAVKQGFQD LGASSLQSAH ELLREKVLRL
EARTGAAQIE GGVHGLVSYE KKSF
//
