IMDH1_YEAST
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 03-AUG-2022, entry version 166.
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; P39567; -.
DR PRIDE; P39567; -.
DR EnsemblFungi; YAR073W_mRNA; YAR073W; YAR073W.
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; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; -; 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; 2.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 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
