ID A0A090X4L7_9FLAO Unreviewed; 490 AA. AC A0A090X4L7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 04-MAR-2015, entry version 4. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964}; 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}; GN Name=guaB {ECO:0000256|HAMAP-Rule:MF_01964}; GN ORFNames=JCM19274_4501 {ECO:0000313|EMBL:GAL78002.1}; OS Algibacter lectus. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Algibacter. OX NCBI_TaxID=221126 {ECO:0000313|EMBL:GAL78002.1}; RN [1] {ECO:0000313|EMBL:GAL78002.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JCM 19274 {ECO:0000313|EMBL:GAL78002.1}; RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K., RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., RA Niwa A., Sawabe T., Sawabe T.; RT "Draft Genome Sequences of Marine Flavobacterium Algibacter lectus RT Strains SS8 and NR4."; RL Genome Announc. 2:e01168-14(2014). 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 -!- 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 -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01964}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000256|HAMAP- CC Rule:MF_01964}. CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000256|HAMAP- CC 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:GAL78002.1}. 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; BBNU01000002; GAL78002.1; -; Genomic_DNA. DR UniPathway; UPA00601; UER00295. DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP. PE 3: Inferred from homology; KW CBS domain {ECO:0000256|HAMAP-Rule:MF_01964}; KW GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01964}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01964}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01964, KW ECO:0000313|EMBL:GAL78002.1}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_01964}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01964}. FT DOMAIN 97 153 CBS 1. {ECO:0000256|HAMAP-Rule:MF_01964}. FT DOMAIN 157 214 CBS 2. {ECO:0000256|HAMAP-Rule:MF_01964}. FT NP_BIND 301 303 NAD. {ECO:0000256|HAMAP-Rule:MF_01964}. FT REGION 341 343 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964}. FT REGION 364 365 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964}. FT REGION 388 392 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964}. FT ACT_SITE 308 308 Thioimidate intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT METAL 303 303 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT METAL 305 305 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT METAL 308 308 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT METAL 473 473 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT METAL 474 474 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT METAL 475 475 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 BINDING 419 419 IMP. {ECO:0000256|HAMAP-Rule:MF_01964}. SQ SEQUENCE 490 AA; 52108 MW; 6875B10DE404887F CRC64; MTAHENKIVG EGLTYDDVLL VPAFSEVLPR EVSIQTKFTR NITINVPIIS AAMDTVTESK MAIAMAQEGG IGVLHKNMSI EAQALKVRRV KRAESGMIID PVTLPVTAVV SDAKKYMAEY SIGGIPIVAE DGTLKGIVTN RDLRFEHNGK RAISEVMTSE KLVTASVGTS LKDAELILQE HKIEKLLIVD DNFKLSGLIT FRDITKLSQK PNANKDQYGR LRVAAALGVT ADAVERAEAL VNAGVDAVVI DTAHGHTKGV VSVLKTIKAK FPNLDVIVGN IATGAAAKYL VEAGADAVKV GIGPGSICTT RVVAGVGFPQ FSAVLEVAAA IKGSGVPVIA DGGIRYTGDI PKAIAAGADT VMLGSLLAGT KESPGETIIY EGRKFKSYRG MGSVEAMKEG SKDRYFQDVE DDIKKLVPEG IVGRVPYKGD LYESIHQFIG GLRAGMGYCG AKDIETLKET GQFVKITASG INESHPHDVT ITKESPNYSR //