ID A0A1B9AXB3_9BACI Unreviewed; 488 AA. AC A0A1B9AXB3; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 27-SEP-2017, entry version 7. 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., RA Wang J., 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) 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: Inosine 5'-phosphate + NAD(+) + H(2)O = CC xanthosine 5'-phosphate + NADH. {ECO:0000256|HAMAP-Rule:MF_01964, CC ECO:0000256|RuleBase:RU003928}. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01964}; CC -!- ENZYME 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: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|PROSITE-ProRule:PRU00703}; KW Complete proteome {ECO:0000313|Proteomes:UP000092673}; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000092673}. FT DOMAIN 95 156 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 157 215 CBS. {ECO:0000259|PROSITE:PS51371}. FT NP_BIND 251 253 NAD. {ECO:0000256|PIRSR:PIRSR000130-3}. FT NP_BIND 301 303 NAD. {ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-3}. FT REGION 341 343 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964, ECO:0000256|PIRSR:PIRSR000130- FT 2}. FT REGION 364 365 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964, ECO:0000256|PIRSR:PIRSR000130- FT 2}. FT REGION 388 392 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964, ECO:0000256|PIRSR:PIRSR000130- FT 2}. FT ACT_SITE 308 308 Thioimidate intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1}. FT ACT_SITE 404 404 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01964, ECO:0000256|PIRSR:PIRSR000130- FT 1}. FT METAL 303 303 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 305 305 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 308 308 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 251 251 NAD. {ECO:0000256|HAMAP-Rule:MF_01964}. FT BINDING 306 306 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 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 //