ID A0A355Q2K0_9DELT Unreviewed; 491 AA. AC A0A355Q2K0; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 05-JUN-2019, entry version 5. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928}; DE Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964}; DE Short=IMPD {ECO:0000256|HAMAP-Rule:MF_01964}; DE Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_01964}; DE EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928}; GN Name=guaB {ECO:0000256|HAMAP-Rule:MF_01964}; GN ORFNames=DDZ97_01295 {ECO:0000313|EMBL:HBM51707.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:HBM51707.1}; RN [1] {ECO:0000313|EMBL:HBM51707.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA10388 {ECO:0000313|EMBL:HBM51707.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) CC to xanthosine 5'-phosphate (XMP), the first committed and rate- CC limiting step in the de novo synthesis of guanine nucleotides, and CC therefore plays an important role in the regulation of cell CC growth. {ECO:0000256|HAMAP-Rule:MF_01964}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; CC Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01964, ECO:0000256|RuleBase:RU003928}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01964}; CC -!- ACTIVITY REGULATION: Mycophenolic acid (MPA) is a non-competitive CC inhibitor that prevents formation of the closed enzyme CC conformation by binding to the same site as the amobile flap. In CC contrast, mizoribine monophosphate (MZP) is a competitive CC inhibitor that induces the closed conformation. MPA is a potent CC inhibitor of mammalian IMPDHs but a poor inhibitor of the CC bacterial enzymes. MZP is a more potent inhibitor of bacterial CC IMPDH. {ECO:0000256|HAMAP-Rule:MF_01964}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; CC XMP from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01964, CC ECO:0000256|RuleBase:RU003928}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01964}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000256|HAMAP- CC Rule:MF_01964, ECO:0000256|RuleBase:RU003927}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01964}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:HBM51707.1}. 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 EMBL; DNZT01000034; HBM51707.1; -; Genomic_DNA. DR UniPathway; UPA00601; UER00295. DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule. 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; IPR005990; IMP_DH. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR Pfam; PF00571; CBS; 2. 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 {ECO:0000256|PROSITE-ProRule:PRU00703}; KW GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964, KW ECO:0000256|RuleBase:RU003928}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01964, KW ECO:0000256|RuleBase:RU003928}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-3, KW ECO:0000256|RuleBase:RU003928}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01964, KW ECO:0000256|RuleBase:RU003927}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_01964, KW ECO:0000256|PIRSR:PIRSR000130-4, ECO:0000256|RuleBase:RU003928}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964, KW ECO:0000256|RuleBase:RU003928}. FT DOMAIN 94 149 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 153 212 CBS. {ECO:0000259|PROSITE:PS51371}. FT NP_BIND 249 251 NAD. {ECO:0000256|PIRSR:PIRSR000130-3}. FT NP_BIND 299 301 NAD. {ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-3}. FT REGION 339 341 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964, ECO:0000256|PIRSR:PIRSR000130- FT 2}. FT REGION 362 363 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964, ECO:0000256|PIRSR:PIRSR000130- FT 2}. FT REGION 386 390 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964, ECO:0000256|PIRSR:PIRSR000130- FT 2}. FT ACT_SITE 306 306 Thioimidate intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1}. FT ACT_SITE 402 402 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01964, ECO:0000256|PIRSR:PIRSR000130- FT 1}. FT METAL 301 301 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 303 303 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 306 306 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 470 470 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT METAL 471 471 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT METAL 472 472 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT BINDING 249 249 NAD. {ECO:0000256|HAMAP-Rule:MF_01964}. FT BINDING 304 304 IMP. {ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2}. FT BINDING 416 416 IMP. {ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2}. SQ SEQUENCE 491 AA; 53179 MW; 517FCAE4331004B6 CRC64; MLQNRITEGL TFDDVLLVPA YSDILPHEVS VQTRLTRHLD CNIPLLSAAM DTVTEHQVAI SMAQEGGLGV IHKNMSVEEQ AAQVDRVKRS ESGMISDPIT VEPEQPLKDA LQLMERYRIS GVPVTRGTEL VGILTNRDLR FETNLDQKVG SVMTSGRDRL VTVSPGIDLE EAKTLLHAHR IEKLLVVSEG YDLLGLITIK DIEKSRKYPN ANKDDRGRLR VGAAVSTSRD LMERTAALIS KGVDLVVLDT AHGHSSKVLQ SIRELRETFP ELEIVAGNIA TASGCEALIK AGVDAVKIGI GPGSICTTRV VAGIGVPQIT AISESASVAR RYGIPVIADG GIKYSGDIVK ALAAGADSVM IGSLFAGTAE TPGQVILYQG RRYKLYRGMG SMGAMKEGSK DRYFQNNIEE SKLVPEGIEG RVPFKGSLAE MVYQFVGGLR SGMGYTGCRN ITELQEQAQF VRITSAGLRE SHVHDVLITE EAPNYPISQV E //