ID   IMDH2_YEAST             Reviewed;         523 AA.
AC   P38697;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   16-JUN-2009, entry version 83.
DE   RecName: Full=Inosine-5'-monophosphate dehydrogenase IMD2;
DE            Short=IMP dehydrogenase;
DE            Short=IMPDH;
DE            Short=IMPD;
DE            EC=1.1.1.205;
GN   Name=IMD2; Synonyms=PUR5; OrderedLocusNames=YHR216W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=94378003; PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
RA   Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
RA   Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
RA   Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
RA   Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
RA   Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
RA   Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
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   -!- INTERACTION:
CC       P43582:-; NbExp=1; IntAct=EBI-9186, EBI-22766;
CC       Q02821:SRP1; NbExp=1; IntAct=EBI-9186, EBI-1797;
CC   -!- MISCELLANEOUS: Present with 7870 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC   -!- SIMILARITY: Contains 2 CBS domains.
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DR   EMBL; U00029; AAB69728.1; -; Genomic_DNA.
DR   PIR; S48997; S48997.
DR   RefSeq; NP_012088.1; -.
DR   HSSP; P12268; 1B3O.
DR   DIP; DIP:2840N; -.
DR   IntAct; P38697; 50.
DR   PRIDE; P38697; -.
DR   Ensembl; YHR216W; Saccharomyces cerevisiae.
DR   GeneID; 856626; -.
DR   GenomeReviews; U00093_GR; YHR216W.
DR   KEGG; sce:YHR216W; -.
DR   NMPDR; fig|4932.3.peg.3265; -.
DR   CYGD; YHR216w; -.
DR   SGD; S000001259; IMD2.
DR   HOGENOM; P38697; -.
DR   OMA; P38697; SIPCVAS.
DR   BRENDA; 1.1.1.205; 250.
DR   NextBio; 982568; -.
DR   GermOnline; YHR216W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; TAS:SGD.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006183; P:GTP biosynthetic process; TAS:SGD.
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   1: Evidence at protein level;
KW   CBS domain; Complete proteome; GMP biosynthesis; Metal-binding; NAD;
KW   Oxidoreductase; Potassium; Purine biosynthesis; Repeat.
FT   CHAIN         1    523       Inosine-5'-monophosphate dehydrogenase
FT                                IMD2.
FT                                /FTId=PRO_0000093682.
FT   DOMAIN      121    183       CBS 1.
FT   DOMAIN      184    240       CBS 2.
FT   NP_BIND     257    280       NAD (By similarity).
FT   ACT_SITE    335    335       Thioimidate intermediate (By similarity).
FT   METAL       330    330       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       332    332       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     280    280       Inhibitor (By similarity).
FT   BINDING     337    337       Inhibitor (By similarity).
FT   BINDING     368    368       IMP (By similarity).
FT   BINDING     415    415       IMP (By similarity).
SQ   SEQUENCE   523 AA;  56530 MW;  7CA3EC11238906B9 CRC64;
     MAAIRDYKTA LDFTKSLPRP DGLSVQELMD SKIRGGLTYN DFLILPGLVD FASSEVSLQT
     KLTRNITLNI PLVSSPMDTV TESEMATFMA LLGGIGFIHH NCTPEDQADM VRRVKNYENG
     FINNPIVISP TTTVGEAKSM KEKYGFAGFP VTTDGKRNAK LVGVITSRDI QFVEDNSLLV
     QDVMTKNPVT GAQGITLSEG NEILKKIKKG RLLVVDEKGN LVSMLSRTDL MKNQNYPLAS
     KSANTKQLLC GASIGTMDAD KERLRLLVKA GLDVVILDSS QGNSIFELNM LKWVKESFPG
     LEVIAGNVVT REQAANLIAA GADGLRIGMG TGSICITQEV MACGRPQGTA VYNVCEFANQ
     FGVPCMADGG VQNIGHITKA LALGSSTVMM GGMLAGTTES PGEYFYQDGK RLKAYRGMGS
     IDAMQKTGTK GNASTSRYFS ESDSVLVAQG VSGAVVDKGS IKKFIPYLYN GLQHSCQDIG
     CRSLTLLKNN VQRGKVRFEF RTASAQLEGG VHNLHSYEKR LHN
//