IMDH_LEPIN
ID IMDH_LEPIN Reviewed; 508 AA.
AC Q8F4Q4;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=LA_1986;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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}.
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DR EMBL; AE010300; AAN49185.1; -; Genomic_DNA.
DR RefSeq; NP_712167.1; NC_004342.2.
DR RefSeq; WP_000070955.1; NC_004342.2.
DR AlphaFoldDB; Q8F4Q4; -.
DR SMR; Q8F4Q4; -.
DR STRING; 189518.LA_1986; -.
DR EnsemblBacteria; AAN49185; AAN49185; LA_1986.
DR GeneID; 61141814; -.
DR KEGG; lil:LA_1986; -.
DR PATRIC; fig|189518.3.peg.1979; -.
DR HOGENOM; CLU_022552_2_1_12; -.
DR InParanoid; Q8F4Q4; -.
DR OMA; MGYCGAK; -.
DR UniPathway; UPA00601; UER00295.
DR Proteomes; UP000001408; Chromosome I.
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; -; 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; PTHR11911; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 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; GMP biosynthesis; Metal-binding; NAD; Oxidoreductase;
KW Potassium; Purine biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..508
FT /note="Inosine-5'-monophosphate dehydrogenase"
FT /id="PRO_0000415689"
FT DOMAIN 111..170
FT /note="CBS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT DOMAIN 174..230
FT /note="CBS 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT ACT_SITE 324
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT ACT_SITE 420
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT BINDING 267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT BINDING 317..319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT BINDING 319
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:0000255|HAMAP-Rule:MF_01964"
FT BINDING 321
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:0000255|HAMAP-Rule:MF_01964"
FT BINDING 322
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT BINDING 324
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:0000255|HAMAP-Rule:MF_01964"
FT BINDING 357..359
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT BINDING 380..381
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT BINDING 404..408
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT BINDING 432
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT BINDING 492
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
SQ SEQUENCE 508 AA; 55881 MW; 5D24AEC8D93512FA CRC64;
MSNQTYRDSE YLDGLSGEEL FNLQIGLTYR DFLVLPGFID FHPSEVELET RLTRNIKLKR
PFISSPMDTV TESQMAIAQA LMGGIGIIHY NNTIEEQVAL VEKVKRFENG FITDPVILGP
KNVIRDLDAI KERKGFTGIP VTEDGTRNSK LIGIVTNRDI DFEKNREITL DKVMTTNLIT
GKEGITLQDA NEIIKKSKIG KLPIVDSQGK LVSLVSRSDL KKNKEFPDAS KDERKRLRCG
AAVSTLLESR DRVAALYEAG VDVIIIDSAQ GNSNYQIEMI QFIKKEFKNL DIVAGNVVTR
AQAENLIRAG ADGLRIGMGP GSICITQDTM AVGRAQATAI YQTAKHSAKY DVPVIADGGI
SNIGDIANSL AIGASTCMMG FMFAGTTEAP GEYFYENGIR LKKYRGMASI EAMKAGGDKR
YFNEGQKVKV AQGVSGSVVD RGSILNFIPY LSQGLRLSFQ DMGYKSIPEI HKALRDGKLR
FERRSESAQA QGSVHGLYSF SAPTMRAE
