ID A0A3G6T329_9FLAO Unreviewed; 486 AA. AC A0A3G6T329; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 11-DEC-2019, entry version 4. 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:AZB23782.1}; GN ORFNames=EG339_03660 {ECO:0000313|EMBL:AZB23782.1}; OS Chryseobacterium bernardetii. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=1241978 {ECO:0000313|EMBL:AZB23782.1, ECO:0000313|Proteomes:UP000271193}; RN [1] {ECO:0000313|EMBL:AZB23782.1, ECO:0000313|Proteomes:UP000271193} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G0229 {ECO:0000313|EMBL:AZB23782.1, RC ECO:0000313|Proteomes:UP000271193}; RA Nicholson A.C., Gulvik C.A., Whitney A.M., Humrighouse B.W., Bell M., RA Holmes B., Steigerwalt A., Villarma A., Sheth M., Batra D., Pryor J., RA Bernardet J.-F., Hugo C., Kampfer P., Newman J., Mcquiston J.R.; RT "Proposal to divide the Flavobacteriaceae and reorganize its genera based RT on Amino Acid Identity values calculated from whole genome sequences."; RL Submitted (NOV-2018) 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 --------------------------------------------------------------------------- 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; CP033932; AZB23782.1; -; Genomic_DNA. DR RefSeq; WP_073300399.1; NZ_CP033932.1. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000271193; Chromosome. 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:AZB23782.1}; 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 96..152 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT DOMAIN 156..213 FT /note="CBS" FT /evidence="ECO:0000259|PROSITE:PS51371" FT NP_BIND 250..252 FT /note="NAD" FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3" FT NP_BIND 300..302 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-3" FT REGION 340..342 FT /note="IMP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT REGION 363..364 FT /note="IMP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT REGION 387..391 FT /note="IMP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT ACT_SITE 307 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1" FT ACT_SITE 403 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-1" FT METAL 302 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT METAL 304 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT METAL 307 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-4" FT METAL 469 FT /note="Potassium; via carbonyl oxygen; shared with FT tetrameric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" 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 BINDING 250 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964" FT BINDING 305 FT /note="IMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" FT BINDING 415 FT /note="IMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964, FT ECO:0000256|PIRSR:PIRSR000130-2" SQ SEQUENCE 486 AA; 51921 MW; 356CDD4B3545DA55 CRC64; MSIHNKIVET AITFDDVLLV PSYSEVLPNQ VSLKSRLTDK ITLNVPIVSA AMDTVTEGDL AIALARVGGL GFIHKNMTIA EQAAQVNRVK RSENGMISDP VTLSKDHTLG QAKEMMAKFK ISGLPVVDAD NVLIGIITNR DVKYQENLDM KVEEIMTKEN LITSDKDTNL EKAKEILLKN RVEKLPIVDK DNKLVGLITI KDIDNQLEYP NANKDQNGRL IVGAGVGVGE DTLDRIEALV QAGVDIVAID SAHGHSKGVL DKISEIRKAY PNLDIVGGNI VTAEAAADLI KAGANVLKVG VGPGSICTTR VVAGVGVPQL SAIYNVYEYA KSQNVAVIAD GGIKLSGDIV KAIASGAGAV MLGSLLAGTD EAPGEEIIFQ GRKFKSYQGM GSLSAMKRGG KERYFQSEAK KFVPEGIEGR VPHKGKLEDV IFQLTGGLRA GMGYCGAKDI EALQKDSKLV MITGSGLKES HPHDVIITQE APNYSL //