ID A0A927L0B2_9ACTN Unreviewed; 501 AA. AC A0A927L0B2; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 03-MAY-2023, entry version 2. 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:MBD9723122.1}; GN ORFNames=IHE70_07670 {ECO:0000313|EMBL:MBD9723122.1}; OS Streptomyces caniscabiei. OC Bacteria; Actinomycetota; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=2746961 {ECO:0000313|EMBL:MBD9723122.1, ECO:0000313|Proteomes:UP000661025}; RN [1] {ECO:0000313|EMBL:MBD9723122.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ID-01-6.2a {ECO:0000313|EMBL:MBD9723122.1}; RA Nguyen H.P., Weisberg A.J., Chang J.H., Clarke C.R.; RT "Streptomyces canutascabiei sp. nov., which causes potato common scab and RT is distributed across the world."; RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases. 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:MBD9723122.1}. 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; JACYXT010000002; MBD9723122.1; -; Genomic_DNA. DR Proteomes; UP000661025; Unassembled WGS sequence. DR GO; GO:0016491; F:oxidoreductase activity; 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 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: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|RuleBase:RU003928}; 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 312 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT ACT_SITE 414 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 255 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 305..307 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 307 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 BINDING 309 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 BINDING 310 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 312 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 BINDING 345..347 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 368..369 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 392..396 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 429 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" 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" FT BINDING 485 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 501 AA; 52672 MW; FC734996A8478151 CRC64; MTANVDGVPD KFATLGLTYD DVLLLPGASD MAPDEIDTAS YVSKNVRVNI PLLSAAMDKV TESRMAIAMA RQGGVGVLHR NLSIEDQANQ VDLVKRSESG MVADPITVHP DATLAEADAL CAKFRISGVP VTDGNKKLLG IVTNRDMAFE SDRSRQVREV MTPMPLVTGK VGISGVEAME LLRKHKIEKL PLVDDAGILK GLITVKDFVK AEKYPHAAKD GEGRLLVGAA VGVAGDAFER AQALIENGVD FIVVDTAHGH SRLVGDMVAK IKSNSSGVDV IGGNIATRDG AQALIDAGVD GIKVGVGPGS ICTTRVVAGI GVPQVTAIYE ASLAAKEAGV PVIGDGGLQY SGDIAKALVA GADTVMLGSL LAGCAESPGE LLFINGKQFK SYRGMGSLGA MQSRGDRKSF SKDRYFQEGV ASDEQLVPEG IEGQVPYRGP LSSVVHQLVG GLRQSMFYVG GRTVPDLQAN GRFVRITSAG LKESHPHDIQ MTVEAPNYSR K //