ID A0A090X4L7_9FLAO Unreviewed; 490 AA. AC A0A090X4L7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 11-DEC-2019, entry version 28. 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=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, ECO:0000313|Proteomes:UP000029643}; RN [1] {ECO:0000313|EMBL:GAL78002.1, ECO:0000313|Proteomes:UP000029643} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM19274 {ECO:0000313|Proteomes:UP000029643}; 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., Niwa A., RA Sawabe T., Sawabe T.; RT "Draft Genome Sequences of Marine Flavobacterium Algibacter lectus Strains RT SS8 and NR4."; RL Genome Announc. 2:e01168-14(2014). 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: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 RefSeq; WP_042495518.1; NZ_FOLN01000005.1. DR EnsemblBacteria; GAL78002; GAL78002; JCM19274_4501. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000029643; 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 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, ECO:0000313|EMBL:GAL78002.1}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130- KW 4, ECO:0000256|RuleBase:RU003928}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964, KW ECO:0000256|RuleBase:RU003928}. FT DOMAIN 97..153 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT DOMAIN 157..214 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 473 FT /note="Potassium; via carbonyl oxygen; shared with FT tetrameric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT METAL 474 FT /note="Potassium; via carbonyl oxygen; shared with FT tetrameric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT METAL 475 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 419 FT /note="IMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" 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 //