ID A0A8B8UKT0_SACPA Unreviewed; 523 AA. AC A0A8B8UKT0; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 25-MAY-2022, entry version 2. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928}; DE Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156}; DE Short=IMPD {ECO:0000256|HAMAP-Rule:MF_03156}; DE Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_03156}; DE EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928}; GN Name=IMD {ECO:0000256|HAMAP-Rule:MF_03156}; GN ORFNames=SPAR_A00010 {ECO:0000313|RefSeq:XP_033764409.1}; OS Saccharomyces paradoxus (Yeast) (Saccharomyces douglasii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=27291 {ECO:0000313|RefSeq:XP_033764409.1}; RN [1] {ECO:0000313|RefSeq:XP_033764409.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS432 {ECO:0000313|RefSeq:XP_033764409.1}; RX PubMed=28416820; RA Yue J.X., Li J., Aigrain L., Hallin J., Persson K., Oliver K., RA Bergstrom A., Coupland P., Warringer J., Lagomarsino M.C., Fischer G., RA Durbin R., Liti G.; RT "Contrasting evolutionary genome dynamics between domesticated and wild RT yeasts."; RL Nat. Genet. 49:913-924(2017). RN [2] {ECO:0000313|RefSeq:XP_033764409.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS432 {ECO:0000313|RefSeq:XP_033764409.1}; RA Yue J.-X.; RT "Population-level Yeast Reference Genomes."; RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|RefSeq:XP_033764409.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS432 {ECO:0000313|RefSeq:XP_033764409.1}; RG NCBI Genome Project; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|RefSeq:XP_033764409.1} RP IDENTIFICATION. RC STRAIN=CBS432 {ECO:0000313|RefSeq:XP_033764409.1}; RG RefSeq; RL Submitted (SEP-2021) to UniProtKB. 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:0000256|HAMAP-Rule:MF_03156}. 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:0000256|HAMAP-Rule:MF_03156, CC ECO:0000256|RuleBase:RU003928}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03156}; 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:0000256|HAMAP-Rule:MF_03156}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP CC from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_03156, CC ECO:0000256|RuleBase:RU003928}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03156}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC {ECO:0000256|ARBA:ARBA00005502, ECO:0000256|HAMAP-Rule:MF_03156, CC ECO:0000256|RuleBase:RU003927}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03156}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_033764409.1; XM_033908518.1. 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; 2. 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 {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE- KW ProRule:PRU00703}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}; KW GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_03156, KW ECO:0000256|RuleBase:RU003928}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03156}; KW NAD {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_03156}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_03156}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03156, KW ECO:0000256|RuleBase:RU003928}. FT DOMAIN 121..183 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT DOMAIN 184..240 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT NP_BIND 278..280 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT NP_BIND 328..330 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT REGION 368..370 FT /note="IMP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT REGION 391..392 FT /note="IMP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT REGION 415..419 FT /note="IMP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT ACT_SITE 335 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT ACT_SITE 437 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT METAL 330 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT METAL 332 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT METAL 335 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT METAL 504 FT /note="Potassium; via carbonyl oxygen; shared with FT tetrameric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT BINDING 333 FT /note="IMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT BINDING 449 FT /note="IMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" SQ SEQUENCE 523 AA; 56499 MW; CA58BE61E9A8D819 CRC64; MAAIKDYETA LQFAKSLPRL DGLSVQELMD SKIRGGLTYN DFLILPGLVD FASSEVSLQT KLTRNITLNI PLVSSPMDTV TESEMAIFMA LSGGIGFIHH NCTPEDQADM VRRVKNYENG FINNPIVISP TTTVGEAKSM KKKYGFAGFP VTEDGKRNAK LVGVITSRDI QFVEDDSLLV QDVMTKNPVT GAQGITLSEG NEILKKIKKG RLLIVDEKGK LVSMLSRTDL MKNQNYPLAS KSANTKQLLC GASIGTMDAD KERLRLLVKA GLDVVILDSS QGNSIFQLNM LKWVKESFAG LEVIAGNVVT REQAANLIAA GADGLRIGMG TGSICITQEV MACGRPQGTA VYNVCEFANQ FGVPCMADGG VQNIGHITKA LALGSSTVMM GGMLAGTTES PGEYFYQDGK RLKAYRGMGS IDAMQKTGTK GNASTSRYFS EFDSVLVAQG VSGAVVDKGS IKKFIPYLYN GLQHSCQDIG CRSLTLLKKN VQSGKVRFEF RTASAQLEGG VNNLHSYEKR LHN //