(data stored in SCRATCH9089 zone)

SWISSPROT: IMDH_PASMU

ID   IMDH_PASMU              Reviewed;         487 AA.
AC   Q9L6B7;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   11-DEC-2019, entry version 132.
DE   RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964};
DE            Short=IMP dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964};
DE            Short=IMPD {ECO:0000255|HAMAP-Rule:MF_01964};
DE            Short=IMPDH {ECO:0000255|HAMAP-Rule:MF_01964};
DE            EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_01964};
GN   Name=guaB {ECO:0000255|HAMAP-Rule:MF_01964}; OrderedLocusNames=PM0295;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10873488; DOI=10.1006/mpat.2000.0365;
RA   Fuller T.E., Kennedy M.J., Lowery D.E.;
RT   "Identification of Pasteurella multocida virulence genes in a septicemic
RT   mouse model using signature-tagged mutagenesis.";
RL   Microb. Pathog. 29:25-38(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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:0000255|HAMAP-Rule:MF_01964}.
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:0000255|HAMAP-Rule:MF_01964};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01964};
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:0000255|HAMAP-Rule:MF_01964}.
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC       from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01964}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01964}.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
CC       Rule:MF_01964}.
DR   EMBL; AF237921; AAF68407.1; -; Genomic_DNA.
DR   EMBL; AE004439; AAK02379.1; -; Genomic_DNA.
DR   RefSeq; WP_005725353.1; NC_002663.1.
DR   SMR; Q9L6B7; -.
DR   PRIDE; Q9L6B7; -.
DR   EnsemblBacteria; AAK02379; AAK02379; PM0295.
DR   GeneID; 29389077; -.
DR   KEGG; pmu:PM0295; -.
DR   eggNOG; ENOG4105CP4; Bacteria.
DR   eggNOG; COG0516; LUCA.
DR   eggNOG; COG0517; LUCA.
DR   HOGENOM; HOG000165755; -.
DR   KO; K00088; -.
DR   OMA; SSMGYCG; -.
DR   BioCyc; PMUL272843:G1FZ8-307-MONOMER; -.
DR   UniPathway; UPA00601; UER00295.
DR   Proteomes; UP000000809; Chromosome.
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; cd00381; IMPDH; 1.
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   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;
DR   PRODOM; Q9L6B7.
DR   SWISS-2DPAGE; Q9L6B7.
KW   CBS domain; GMP biosynthesis; Metal-binding; NAD; Oxidoreductase;
KW   Potassium; Purine biosynthesis; Reference proteome; Repeat.
FT   CHAIN           1..487
FT                   /note="Inosine-5'-monophosphate dehydrogenase"
FT                   /id="PRO_0000093703"
FT   DOMAIN          93..149
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   DOMAIN          153..214
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   NP_BIND         248..250
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   NP_BIND         298..300
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   REGION          338..340
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   REGION          361..362
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   REGION          385..389
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   ACT_SITE        305
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   ACT_SITE        401
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           300
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           302
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           305
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           469
FT                   /note="Potassium; via carbonyl oxygen; shared with
FT                   tetrameric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           470
FT                   /note="Potassium; via carbonyl oxygen; shared with
FT                   tetrameric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   METAL           471
FT                   /note="Potassium; via carbonyl oxygen; shared with
FT                   tetrameric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         248
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         303
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         415
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
SQ   SEQUENCE   487 AA;  52008 MW;  0871DB08893B8FCA CRC64;
     MLRVIKEALT FDDVLLVPAH STVLPNTADL STQLTKTIRL NIPMLSAAMD TVTETKLAIS
     LAQEGGIGFI HKNMSIERQA ERVRKVKKFE SGIVSDPVTV SPTLSLAELS ELVKKNGFAS
     FPVVDDEKNL VGIITGRDTR FVTDLNKTVA DFMTPKARLV TVKRNASRDE IFGLMHTHRV
     EKVLVVSDDF KLKGMITLKD YQKSEQKPQA CKDEFGRLRV GAAVGAGPGN EERIDALVKA
     GVDVLLIDSS HGHSEGVLQR VRETRAKYPD LPIVAGNVAT AEGAIALADA GASAVKVGIG
     PGSICTTRIV TGVGVPQITA IADAAEALKD RGIPVIADGG IRFSGDISKA IAAGASCVMV
     GSMFAGTEEA PGEIELYQGR AFKSYRGMGS LGAMSKGSSD RYFQSDNAAD KLVPEGIEGR
     IPYKGFLKEI IHQQMGGLRS CMGLTGCATI DELRTKAQFV RISGAGIQES HVHDVTITKE
     APNYRMG
//

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