SPM_002485
  | Uniprot: A0A037UND2
Description: inosine-5-monophosphate dehydrogenase EC number: 1.1.1.205 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928}. Cofactor: COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-Rule:MF_01964}; Enzyme regulation: ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH. {ECO:0000256|HAMAP-Rule:MF_01964}. Function [CC]: FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. {ECO:0000256|HAMAP-Rule:MF_01964}. Pathway: PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928}. Active site: ACT_SITE 302 302 Thioimidate intermediate. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-1}.; ACT_SITE 398 398 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-1}. Binding site: BINDING 245 245 NAD. {ECO:0000256|HAMAP-Rule:MF_01964}.; BINDING 300 300 IMP. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-2}.; BINDING 410 410 IMP. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-2}. Calcium binding: DNA binding: Metal binding: METAL 297 297 Potassium; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-4}.; METAL 299 299 Potassium; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-4}.; METAL 302 302 Potassium; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-4}.; METAL 464 464 Potassium; via carbonyl oxygen; shared with tetrameric partner. {ECO:0000256|HAMAP-Rule:MF_01964}.; METAL 465 465 Potassium; via carbonyl oxygen; shared with tetrameric partner. {ECO:0000256|HAMAP-Rule:MF_01964}.; METAL 466 466 Potassium; via carbonyl oxygen; shared with tetrameric partner. {ECO:0000256|HAMAP-Rule:MF_01964}. Nucleotide binding: NP_BIND 245 247 NAD. {ECO:0000256|PIRSR:PIRSR000130-3}.; NP_BIND 295 297 NAD. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-3}. Site: Gene names (primary): guaB Gene names (synonym): Mass: 52,185 Subunit structure [CC]: SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01964}. Gene ontology (GO): IMP dehydrogenase activity [GO:0003938]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; GMP biosynthetic process [GO:0006177] Gene ontology IDs: GO:0000166; GO:0003938; GO:0006177; GO:0046872 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003927}.; SIMILARITY: Contains 2 CBS domains. {ECO:0000256|HAMAP-Rule:MF_01964}. Protein families: IMPDH/GMPR family Coiled coil: Domain [FT]: DOMAIN 91 149 CBS. {ECO:0000259|PROSITE:PS51371}.; DOMAIN 151 211 CBS. {ECO:0000259|PROSITE:PS51371}. Motif: Region: REGION 335 337 IMP binding. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-2}.; REGION 358 359 IMP binding. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-2}.; REGION 382 386 IMP binding. {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-2}. EMBL: AGBZ02000001 ProteinModelPortal: A0A037UND2 MEROPS: EnsemblBacteria KO: KAI92882 UniPathway: CDD: Gene3D: cd00381 HAMAP: 3.20.20.70 InterPro: MF_01964 PANTHER: IPR013785;IPR000644;IPR005990;IPR015875;IPR001093 PIRSF: PTHR11911:SF6 PRINTS: PIRSF000130 PROSITE: Pfam: PS51371;PS00487 ProDom: PF00571;PF00478 SMART: SUPFAM: SM00116 TIGRFAMs: |
463168-464614(-) >nucleotide sequence TAAACCATTATTTGAAATTTCCACAAACTGAGCTGTTTTTTGTAACATTAAAATATTTTT TGCACCACAATAACCAAAACCGCTTCGTACACCACCAATAAATTGAAATAAAATATCACT TAATTTACCTTTTAATAAAACTCGTCCTTCAACTCCTTCTGGAACTAATTTACGATTCTT ATCTTGAAAATAACGATCAGCACTACCTTTTTTCATAGCAGCTAATGAACCCATTCCCAT ATATGTTTTATATTTTTTACCTTCAACAATCATTTCTTCACCGGGTGCTTCAAATGTTGA AGCAAAAACTGAACCCATCATTACAGCATTAGCACCAGCTGCAAGTGCTTTAACAACATC ACCAGAATATTTAATTCCACCATCAGCAATGACTGGAATTTCTTTTCCTTTGCAAGCCTC ATAGACATCATTAATAGCTGTCATTTGAGGAACTCCAACTCCAGCAACAACTCTTGTTGT ACAAATACTTCCTGGCCCGACACCAACTTTAATTGCATTAGCACCAGCTGCAATTAAATC TAACGCTCCTTGAGCAGTAACAACATTCCCAACGATTAAATCAATGGTTGGAAAAGCTTT TCTAATTTTTTGAACCATATTAATAATACCTTGACTATGACCGTGTGCTGAATCAACAAC AATTACATCAACTCCAACTGCAACAAGTTTTTCAACACGTAATAATGTACTTTCATCAAT TCCAACTGCTGCACCAACTCGTAATCGCCCTTGTTCATCTTTACAAGCATTAGGATATTC ATCACGATTATTAATATCTTTAATGGTAATTAACCCAGTTAAAATATTTTTTTCATTAAC AATTGGCAGTTTTTCAATACGATTATTTAACAAAATATCTTTTGCTTGCTCTAAATCAAT ATTTTCATGAGTTGTAATCAAGTTTTTTACAGTCATAAATTTATCAACCGAAGCAGTTAA ATCATGACATGCTCTAATATCACGATTTGTAATTATTCCTAATAATTTGTTTTCTTCATC AACAATTGGCAGACCCGAAATACGATACTGAGCCATAATATTTTCAGCATCCTGAACAGT CATTGTTGGTTTTAATGTTATTGGATTAATAATAAAACCGGATTCATTACGTTTAACTTT TTCAACTTCTGCCGCTTGTTTATCAATTGATAAATTTTTATGAATAATTCCAATACCACC TTCGCGAGCAATTGCAATTGCCAATTTTGATTCAGTAACAGTATCCATTGCTGAAGATAT AAAAGGAATATTTAACTCAATATTTTTTGTTAATTTAGTTCTTAAATCAATCTGATATGG CAAAATATCTGATTTTTGTGGAACTAATAGTAGATCATCAAAGGTATAAGATTTTTTAAT TTGCAT >protein sequence REGGIGIIHKNLSIDKQAAEVEKVKRNESGFIINPITLKPTMTVQDAENIMAQYRISGLP IVDEENKLLGIITNRDIRACHDLTASVDKFMTVKNLITTHENIDLEQAKDILLNNRIEKL PIVNEKNILTGLITIKDINNRDEYPNACKDEQGRLRVGAAVGIDESTLLRVEKLVAVGVD VIVVDSAHGHSQGIINMVQKIRKAFPTIDLIVGNVVTAQGALDLIAAGANAIKVGVGPGS ICTTRVVAGVGVPQMTAINDVYEACKGKEIPVIADGGIKYSGDVVKALAAGANAVMMGSV FASTFEAPGEEMIVEGKKYKTYMGMGSLAAMKKGSADRYFQDKNRKLVPEGVEGRVLLKG KLSDILFQFIGGVRSGFGYCGAKNILMLQKTAQFVEISNNGLKESHPHDIAITKEPPNYT K |
© Fisunov Lab of Proteomics, 2016.