ID A0A3G6T329_9FLAO Unreviewed; 486 AA. AC A0A3G6T329; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 10-APR-2019, entry version 2. 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 RT based on Amino Acid Identity values calculated from whole genome RT sequences."; RL Submitted (NOV-2018) 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: CC Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; CC Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01964, ECO:0000256|RuleBase:RU003928}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01964}; CC -!- ACTIVITY 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 --------------------------------------------------------------------------- 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 UniPathway; UPA00601; UER00295. DR Proteomes; UP000271193; Chromosome. 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:UP000271193}; 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|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, KW ECO:0000256|RuleBase:RU003928}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964, KW ECO:0000256|RuleBase:RU003928}. FT DOMAIN 96 152 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 156 213 CBS. {ECO:0000259|PROSITE:PS51371}. FT NP_BIND 300 302 NAD. {ECO:0000256|HAMAP-Rule:MF_01964}. FT REGION 340 342 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964}. FT REGION 363 364 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964}. FT REGION 387 391 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_01964}. FT ACT_SITE 307 307 Thioimidate intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT ACT_SITE 403 403 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01964}. FT METAL 302 302 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT METAL 304 304 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT METAL 307 307 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01964}. FT METAL 469 469 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000256|HAMAP-Rule:MF_01964}. 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 BINDING 250 250 NAD. {ECO:0000256|HAMAP-Rule:MF_01964}. FT BINDING 305 305 IMP. {ECO:0000256|HAMAP-Rule:MF_01964}. FT BINDING 415 415 IMP. {ECO:0000256|HAMAP-Rule:MF_01964}. 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 //