ID PUR9_RHOSK Reviewed; 529 AA. AC B9KP36; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 15-DEC-2009, entry version 9. DE RecName: Full=Bifunctional purine biosynthesis protein purH; DE Includes: DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase; DE EC=2.1.2.3; DE AltName: Full=AICAR transformylase; DE Includes: DE RecName: Full=IMP cyclohydrolase; DE EC=3.5.4.10; DE AltName: Full=Inosinicase; DE AltName: Full=IMP synthetase; DE AltName: Full=ATIC; GN Name=purH; OrderedLocusNames=RSKD131_2498; OS Rhodobacter sphaeroides (strain KD131 / KCTC 12085). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=557760; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19028901; DOI=10.1128/JB.01565-08; RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., RA Lee J.K.; RT "Complete genome sequence of Rhodobacter sphaeroides KD131."; RL J. Bacteriol. 191:1118-1119(2009). CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + 5-amino-1-(5- CC phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. CC -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl CC THF route): step 1/1. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamide: step 1/1. CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal CC region (By similarity). CC -!- SIMILARITY: Belongs to the purH family. 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; CP001150; ACM02358.1; -; Genomic_DNA. DR RefSeq; YP_002526859.1; -. DR GeneID; 7359196; -. DR GenomeReviews; CP001150_GR; RSKD131_2498. DR KEGG; rsk:RSKD131_2498; -. DR OMA; VVKHVKS; -. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:HAMAP. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide for...; IEA:HAMAP. DR GO; GO:0006188; P:IMP biosynthetic process; IEA:InterPro. DR HAMAP; MF_00139; -; 1. DR InterPro; IPR002695; AICARFT_IMPCHas. DR InterPro; IPR013982; AICARFT_IMPCHas_formly. DR InterPro; IPR011607; MGS. DR PANTHER; PTHR11692; AICARFT_IMPCHas; 1. DR Pfam; PF01808; AICARFT_IMPCHas; 1. DR Pfam; PF02142; MGS; 1. DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1. DR SMART; SM00798; AICARFT_IMPCHas; 1. DR SMART; SM00851; MGS; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Multifunctional enzyme; KW Purine biosynthesis; Transferase. FT CHAIN 1 529 Bifunctional purine biosynthesis protein FT purH. FT /FTId=PRO_1000122969. SQ SEQUENCE 529 AA; 55829 MW; 085069F91C150C9C CRC64; MTNLVPVGRA LLSVSDKSGL LDLARALADL EVELISTGGT AAALRAAGLK VRDVAEVTGF PEMMDGRVKT LHPMVHGGLL ALRDDDEHLV AMAAHGIEPI DLLVVNLYPF EAAVARGASY DDCIENIDIG GPAMIRAAAK NHRFVNVVTD TADYKALLDE LRAHDGATRL SFRQKLALTA YARTAAYDTA VSTWMAGALK AEAPRRRSFA GTLAQTMRYG ENPHQKAAFY TDGSARPGVA TAKQWQGKEL SYNNINDTDA AFELVAEFDP AEGPACVIVK HANPCGVARG ATLAEAYARA FDCDRVSAFG GIIALNQPLD AATAEKITEI FTEVVIAPGA DEEARAIFAA KKNLRLLTTE ALPDPLAPGL AFKQVAGGFL VQDRDAGHVD ALDLKVVTKR APSDAELADL LFAWTVAKHV KSNAIVYVKD GATVGVGAGQ MSRVDSTRIA ARKSQDMAQA LGLAQPLTQG SVVASDAFFP FADGLLAAAE AGATAIIQPG GSMRDDEVIA AADEAGLAMV FTGQRHFRH //