ID PUR9_ALCBS Reviewed; 525 AA. AC Q0VMY5; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 25. 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=ABO_2015; OS Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., RA Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., RA Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., RA Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A., RA Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., RA Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine RT bacterium Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(2006). 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 http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM286690; CAL17463.1; -; Genomic_DNA. DR RefSeq; YP_693735.1; -. DR GeneID; 4211146; -. DR GenomeReviews; AM286690_GR; ABO_2015. DR KEGG; abo:ABO_2015; -. DR NMPDR; fig|393595.12.peg.2017; -. DR HOGENOM; Q0VMY5; -. DR OMA; Q0VMY5; VVKHVKS. DR BioCyc; ABOR393595:ABO_2015-MON; -. 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 TIGRFAMs; TIGR00355; purH; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Multifunctional enzyme; KW Purine biosynthesis; Transferase. FT CHAIN 1 525 Bifunctional purine biosynthesis protein FT purH. FT /FTId=PRO_1000057892. SQ SEQUENCE 525 AA; 56122 MW; 4C40FF4E3C0E576D CRC64; MSNVERALIS VSDKTGIVEF AQALADKGVE LLSTGGTFKK LQEAGIAVRE VSDYTGFPEM MAGRVKTLHP KVHGGILGRR GQDEQVMADN DISPIDLVVV NLYPFEATVA NPDCSLEDAI ENIDIGGPTM VRSAAKNNAS VGIVTDAADY QRVLDDMAAN NGALSDDLRF DLAIKAFEHT AAYDSAIANY FGKKVEGQDG MSNLDFPRTI NLNFEKTQNM RYGENPHQKA AFYTERNPAP ASIATAKQLQ GKELSYNNIA DTDAALECVK GFTKPACVIV KHANPCGVAV SLDGITTAYD LAFATDTESA FGGIIAFNRK LDAATAQAIV DRQFVEVIIA PSATEEALAI TAAKKNVRVL VCGEMEGVAA SGLDYKRVNG GLLVQDRDLG MITEGELKVV TKRAPTEAEM HDLIFAWKVA KFVKSNAIVY AKDRQTVGVG AGQMSRVNSA RIAAIKAEHA GLQVKGSVMA SDAFFPFRDG IDNAAKVGIS CVIQPGGSIR DEEVIAAADE AGMAMVFTGM RHFRH //