ID A0A1B9AXB3_9BACI Unreviewed; 488 AA. AC A0A1B9AXB3; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 12-AUG-2020, entry version 13. 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=A8L44_18290 {ECO:0000313|EMBL:OCA88383.1}; OS Bacillus sp. FJAT-27986. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1743146 {ECO:0000313|EMBL:OCA88383.1, ECO:0000313|Proteomes:UP000092673}; RN [1] {ECO:0000313|EMBL:OCA88383.1, ECO:0000313|Proteomes:UP000092673} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-27986 {ECO:0000313|EMBL:OCA88383.1, RC ECO:0000313|Proteomes:UP000092673}; RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Q., Zhu Y., Wang J., RA Liu B., Liu G.; RT "Bacillus sp. FJAT-27986."; RL Submitted (MAY-2016) 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. CC {ECO:0000256|ARBA:ARBA00005502, ECO:0000256|HAMAP-Rule:MF_01964, CC 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:OCA88383.1}. 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; MAYV01000007; OCA88383.1; -; Genomic_DNA. DR RefSeq; WP_066103306.1; NZ_MAYV01000007.1. DR EnsemblBacteria; OCA88383; OCA88383; A8L44_18290. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000092673; 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; 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|ARBA:ARBA00023122, ECO:0000256|PROSITE- KW ProRule:PRU00703}; KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP- KW Rule:MF_01964, ECO:0000256|RuleBase:RU003928}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01964, 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|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01964, ECO:0000256|RuleBase:RU003927}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01964, KW ECO:0000256|PIRSR:PIRSR000130-4, ECO:0000256|RuleBase:RU003928}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_01964, ECO:0000256|RuleBase:RU003928}; KW Reference proteome {ECO:0000313|Proteomes:UP000092673}. FT DOMAIN 95..156 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT DOMAIN 157..215 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT NP_BIND 251..253 FT /note="NAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3" FT NP_BIND 301..303 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-3" FT REGION 341..343 FT /note="IMP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT REGION 364..365 FT /note="IMP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT REGION 388..392 FT /note="IMP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT ACT_SITE 308 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1" FT ACT_SITE 404 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1" FT METAL 303 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT METAL 305 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT METAL 308 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT METAL 470 FT /note="Potassium; via carbonyl oxygen; shared with FT tetrameric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT METAL 471 FT /note="Potassium; via carbonyl oxygen; shared with FT tetrameric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT METAL 472 FT /note="Potassium; via carbonyl oxygen; shared with FT tetrameric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 251 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 306 FT /note="IMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 416 FT /note="IMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" SQ SEQUENCE 488 AA; 53087 MW; 5086ED0AF5ED632C CRC64; MWKDKFSKEG LTFDDVLLIP GKSEVLPKDV SLKVSLADNL ALNIPIISAG MDTVTESEMA IAMARQGGLG VIHKNMSIEQ QAEQVDKVKR SENGVITKPF FLTPENQVYD AEHLMGKYRI SGVPIVNNKE EKKLVGIITN RDMRFIRDYS MRIDDVMTKE NLVTAPVGTN LEEAQKILQQ YKIEKLPLVD EEGTLQGLIT IKDIEKIIEF PRSAKDKYGR LLVAAAVGVT SDTMKRVEML VSADVDAIVL DTAHGHSKGV LDKVREIRET FPELTIIAGN VATAEGTRAL IEAGADIVKV GIGPGSICTT RVVAGVGVPQ ITAIYDCATE ARKHGKSIIA DGGIKYSGDV AKALAAGGHA VMLGSLLAGV TESPGDTEIF QGRRFKVYRG MGSVAAMEKG SKDRYFQEDA KKFVPEGIEG RIPYKGPLAD TIYQLIGGLR AGMGYCGTKD LEELRENSQF VRMTGAGLKE SHPHDVQITK EAPNYSYN //