ID A0A927BLZ1_STRGL Unreviewed; 500 AA. AC A0A927BLZ1; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 13-SEP-2023, entry version 4. 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 ECO:0000313|EMBL:MBD2829090.1}; GN ORFNames=ID875_13580 {ECO:0000313|EMBL:MBD2829090.1}; OS Streptomyces globisporus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1908 {ECO:0000313|EMBL:MBD2829090.1, ECO:0000313|Proteomes:UP000616788}; RN [1] {ECO:0000313|EMBL:MBD2829090.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=QF2 {ECO:0000313|EMBL:MBD2829090.1}; RA Montano E.T., Nideffer J.F., Brumage L., Erb M., Derman A.I., Davis J.P., RA Estrada E., Fu S., Le D., Vuppala A., Tran C., Luterstein E., Lakkaraju S., RA Panchagnula S., Ren C., Doan J., Tran S., Soriano J., Fujita Y., Gutala P., RA Fujii Q., Lee M., Bui A., Villarreal C., Shing S.R., Kim S., Freeman D., RA Racha V., Ho A., Kumar P., Falah K., Dawson T., Enustun E., Prichard A., RA Gomez A., Khanna K., Trigg S., Fernandez L., Pogliano K., Pogliano J.; RT "Isolation and characterization of Streptomyces bacteriophages and RT Streptomyces strains encoding biosynthetic arsenals: Streptomyces strains RT and phages for antibiotic discovery."; RL PLoS ONE 0:0-0(2020). 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_01964}. 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_01964, CC ECO:0000256|RuleBase:RU003928}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01964}; 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_01964}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP CC 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 of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01964}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBD2829090.1}. 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; JACWUS010000001; MBD2829090.1; -; Genomic_DNA. DR Proteomes; UP000616788; Unassembled WGS sequence. 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; cd04601; CBS_pair_IMPDH; 1. DR CDD; cd00381; IMPDH; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR01302; IMP_dehydrog; 1. 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 3: Inferred from homology; KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE- KW ProRule:PRU00703}; KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP- KW Rule:MF_01964}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01964}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01964}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01964}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964, KW ECO:0000256|RuleBase:RU003928}. FT DOMAIN 101..157 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT DOMAIN 161..218 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT ACT_SITE 311 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1" FT ACT_SITE 413 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1" FT BINDING 255..257 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3" FT BINDING 255 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 304..306 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-3" FT BINDING 306 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT BINDING 308 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT BINDING 309 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 311 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT BINDING 344..346 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 367..368 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 391..395 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 428 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 482 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 483 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 484 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" SQ SEQUENCE 500 AA; 52406 MW; 44E406810A234E4A CRC64; MTANVDGVPE KFATLGLTYD DVLLLPGASE VLPNAVDTSS LISRNVRVNI PLLSAAMDKV TEARMAIAMA RQGGVGVLHR NLSIEDQVNQ VDLVKRSESG MVTDPITVHP DATLAEADAL CAKFRISGVP VTDGAGKLLG IVTNRDMAFE SDRSRQVREV MTPMPLVTGR VGISGVEAME LLRRHKIEKL PLVDEAGLLK GLITVKDFKK AEQYPNAAKD ADGRLLVGAA VGASPEALDR AQALAAAGVD FLIVDTSHGH NRNALDWMAK IKSSVGVDVI GGNVATRDGA QALIDAGVDG VKVGVGPGSI CTTRVVAGIG VPQVTAIYEA ALAARAAGVP VIGDGGLQYS GDIGKALAAG ADSVMLGSLL AGCEESPGEL MFINGKQFKS YRGMGSLGAM QSRGQGRSYS KDRYFQAEVA SDDKLVPEGI EGQVPYRGPL ANVLHQLVGG LRQTMGYVGA ATVDEMESKG RFVRITSAGL KESHPHDIQM TVEAPNYSKK //