Q8FR29PUR9_COREFBifunctional purine biosynthesis protein PurHPhosphoribosylaminoimidazolecarboxamide formyltransferase2.1.2.3AICAR transformylaseIMP cyclohydrolase3.5.4.10ATICIMP synthaseInosinicasepurHCE0937Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)BacteriaActinomycetotaActinomycetesMycobacterialesCorynebacteriaceaeCorynebacteriumComparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA](6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamideH2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamidePurine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.The IMP cyclohydrolase activity resides in the N-terminal region.Belongs to the PurH family.HydrolaseMultifunctional enzymePurine biosynthesisReference proteomeTransferaseMSEDRKAIKRALISVYDKTGLEDLAQALHRAGVEIVSTGSTAAKIADLGIPVTPVEELTGFPECLEGRVKTLHPKVHAGILADTRKDDHLRQLDELGVTPFQLVVVNLYPFAETVASGADFDDCVEQIDIGGPSMVRAAAKNHPSVAVVTSPGQYEDVVSVLNTGGFSRAERTKLAAEAFRHTATYDVTVATWISEQLSAADTELEFPGWIGSTSTLARSLRYGENPHQSAALYVSHGASGLAQATQLHGKEMSYNNYTDSDAAWRAAWDHERPCVAIIKHANPCGIAVSDESIAAAHRQAHACDSVSAFGGVIASNREVSVEMAEQVAEIFTEVIIAPSYEEGAVEVLSQKKNIRILQAEAPVREGFETREISGGLLVQERDLIHAEGDNPANWTLAAGEAVSAEVLKDLEFAWTAVRSVKSNAILLAKDGATVGVGMGQVNRVDSARLAVDRAGEERATGSVAASDAFFPFADGFEVLAQAGITAVVQPGGSIRDDEVIEAANKAGVTMYLTGARHFSH
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