ID   IMDH1_YEAST             Reviewed;         403 AA.
AC   P39567;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-NOV-2023, entry version 169.
DE   RecName: Full=Putative inosine-5'-monophosphate dehydrogenase 1 {ECO:0000305|PubMed:12746440};
DE            Short=IMP dehydrogenase 1 {ECO:0000303|PubMed:12746440};
DE            Short=IMPD 1;
DE            Short=IMPDH 1;
DE            EC=1.1.1.205 {ECO:0000250|UniProtKB:P38697};
GN   Name=IMD1; OrderedLocusNames=YAR073W; ORFNames=FUN63;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RA   Bussey H., Keng T., Storms R.K., Vo D., Zhong W., Fortin N., Barton A.B.,
RA   Kaback D.B., Clark M.W.;
RT   "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 52
RT   Kbp CDC15-FLO1-PHO11-YAR074 region.";
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   IDENTIFICATION AS PSEUDOGENE, AND LACK OF TRANSCRIPT.
RX   PubMed=12746440; DOI=10.1074/jbc.m303736200;
RA   Hyle J.W., Shaw R.J., Reines D.;
RT   "Functional distinctions between IMP dehydrogenase genes in providing
RT   mycophenolate resistance and guanine prototrophy to yeast.";
RL   J. Biol. Chem. 278:28470-28478(2003).
RN   [5]
RP   LACK OF TRANSCRIPT.
RX   PubMed=16582424; DOI=10.1534/genetics.106.058420;
RA   Barton A.B., Kaback D.B.;
RT   "Telomeric silencing of an open reading frame in Saccharomyces
RT   cerevisiae.";
RL   Genetics 173:1169-1173(2006).
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:0000250|UniProtKB:P38697};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:P38697};
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC       from IMP: step 1/1. {ECO:0000250|UniProtKB:P38697}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P38697}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P38697}.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene unlikely to encode a
CC       functional protein. In strain S288c, this gene has a frameshift
CC       compared to the other IMD alleles, producing 2 ORFs YAR073W and
CC       YAR075W. Additionally, YAR073W is not transcribed and lacks the
CC       biological functions of the other IMD genes even when artificially
CC       expressed. Because of that it is not part of the S.cerevisiae S288c
CC       complete/reference proteome set. {ECO:0000305|PubMed:12746440,
CC       ECO:0000305|PubMed:16582424, ECO:0000305|PubMed:24374639}.
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DR   EMBL; L28920; AAC09509.1; -; Genomic_DNA.
DR   PIR; S53477; S53477.
DR   AlphaFoldDB; P39567; -.
DR   SMR; P39567; -.
DR   DIP; DIP-6455N; -.
DR   IntAct; P39567; 9.
DR   MINT; P39567; -.
DR   STRING; 4932.YAR073W; -.
DR   iPTMnet; P39567; -.
DR   MaxQB; P39567; -.
DR   PaxDb; 4932-YAR073W; -.
DR   EnsemblFungi; YAR073W_mRNA; YAR073W; YAR073W.
DR   AGR; SGD:S000000095; -.
DR   SGD; S000000095; IMD1.
DR   eggNOG; KOG2550; Eukaryota.
DR   GeneTree; ENSGT00940000170207; -.
DR   HOGENOM; CLU_022552_2_1_1; -.
DR   UniPathway; UPA00601; UER00295.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd04601; CBS_pair_IMPDH; 1.
DR   CDD; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000130; IMPDH; 1.
DR   SMART; SM00116; CBS; 2.
DR   SMART; SM01240; IMPDH; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   5: Uncertain;
KW   CBS domain; Cytoplasm; GMP biosynthesis; Metal-binding; NAD;
KW   Oxidoreductase; Potassium; Purine biosynthesis; Repeat.
FT   CHAIN           1..403
FT                   /note="Putative inosine-5'-monophosphate dehydrogenase 1"
FT                   /id="PRO_0000093681"
FT   DOMAIN          121..183
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          184..240
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   ACT_SITE        335
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P50097"
FT   BINDING         278..280
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P50097"
FT   BINDING         328..330
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P50097"
FT   BINDING         330
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P50097"
FT   BINDING         332
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P50097"
FT   BINDING         333
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P50097"
FT   BINDING         335
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P50097"
FT   BINDING         368..370
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P50097"
SQ   SEQUENCE   403 AA;  44386 MW;  FEBC13E46D5D1ECD CRC64;
     MAAIRDYKTA LDLTKSLPRP DGLSVQELMD SKIRGGLAYN DFLILPGLVD FASSEVSLQT
     KLTRNITLNI PLVSSPMDTV TESEMATFMA LLDGIGFIHH NCTPEDQADM VRRVKNYENG
     FINNPIVISP TTTVGEAKSM KEKYGFAGFP VTADGKRNAK LVGAITSRDI QFVEDNSLLV
     QDVMTKNPVT GAQGITLSEG NEILKKIKKG RLLVVDEKGN LVSMLSRTDL MKNQKYPLAS
     KSANTKQLLW GASIGTMDAD KERLRLLVKA GLDVVILDSS QGNSIFQLNM IKWIKETFPD
     LEIIAGNVVT KEQAANLIAA GADGLRIGMG TGSICITQKV MACGRPQGTA VYNVCEFANQ
     FGVPCMADGG VQKHWSYYYQ SFGSWFFYCY DGWYVGRYYR ITR
//