ID   IMDH_HELPJ              Reviewed;         481 AA.
AC   Q9ZL14;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Inosine-5'-monophosphate dehydrogenase;
DE            Short=IMP dehydrogenase;
DE            Short=IMPDH;
DE            Short=IMPD;
DE            EC=1.1.1.205;
GN   Name=guaB; OrderedLocusNames=jhp_0768;
OS   Helicobacter pylori J99 (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=99120557; PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G.,
RA   Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C.,
RA   Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F.,
RA   Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human
RT   gastric pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O =
CC       xanthosine 5'-phosphate + NADH.
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
CC       XMP from IMP: step 1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC   -!- SIMILARITY: Contains 2 CBS domains.
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DR   EMBL; AE001439; AAD06347.1; -; Genomic_DNA.
DR   PIR; H71890; H71890.
DR   RefSeq; NP_223486.1; -.
DR   HSSP; P49058; 1EEP.
DR   GeneID; 890128; -.
DR   GenomeReviews; AE001439_GR; jhp_0768.
DR   KEGG; hpj:jhp0768; -.
DR   NMPDR; fig|85963.1.peg.764; -.
DR   HOGENOM; Q9ZL14; -.
DR   OMA; Q9ZL14; CVGLITV.
DR   BioCyc; HPYL85963:JHP0768-MON; -.
DR   BRENDA; 1.1.1.205; 295085.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IEA:EC.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   InterPro; IPR005990; IMP_DH.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   InterPro; IPR018529; IMP_DH_rel.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF00571; CBS; 1.
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;
KW   CBS domain; Complete proteome; GMP biosynthesis; Metal-binding; NAD;
KW   Oxidoreductase; Potassium; Purine biosynthesis; Repeat.
FT   CHAIN         1    481       Inosine-5'-monophosphate dehydrogenase.
FT                                /FTId=PRO_0000093699.
FT   DOMAIN       92    148       CBS 1.
FT   DOMAIN      152    209       CBS 2.
FT   NP_BIND     225    246       NAD (By similarity).
FT   ACT_SITE    300    300       Thioimidate intermediate (By similarity).
FT   METAL       295    295       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       297    297       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     333    333       IMP (By similarity).
FT   BINDING     380    380       IMP (By similarity).
SQ   SEQUENCE   481 AA;  51689 MW;  688262DCD14EFDAB CRC64;
     MRILQRALTF EDVLMVPRKS SVLPKDVSLK SRLTKNIGLN IPFISAAMDT VTEHKTAIAM
     ARLGGIGIVH KNMDIQTQVK EITKVKKSES GVINDPIFIH AHRTLADAKV ITDNYKISGV
     PVVDDKGLLI GILTNRDVRF ETDLSKKVGD VMTKMPLVTA HVGISLDEAS DLMHKHKIEK
     LPIVDKDNVL KGLITIKDIQ KRIEYPEANK DDFGRLRVGA AIGVGQLDRA EMLVKAGVDA
     LVLDSAHGHS ANILHTLEEI KKSLVVDVIV GNVVTKEATS DLISAGADAV KVGIGPGSIC
     TTRIVAGVGM PQVSAIDNCV EVASKFDIPV IADGGIRYSG DVAKALALGA SSVMIGSLLA
     GTEESPGDFM IYQGRQYKSY RGMGSIGAMT KGSSDRYFQE GVASEKLVPE GIEGRVPYRG
     KVSDMIFQLV GGVRSSMGYQ GAKNILELYQ NAEFVEITSA GLKESHVHGV DITKEAPNYY
     G
//