ID PUR9_YERPE Reviewed; 529 AA. AC Q8ZAR3; Q0WAT0; Q8D1H0; DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 137. DE RecName: Full=Bifunctional purine biosynthesis protein PurH {ECO:0000255|HAMAP-Rule:MF_00139}; DE Includes: DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_00139}; DE EC=2.1.2.3 {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=AICAR transformylase {ECO:0000255|HAMAP-Rule:MF_00139}; DE Includes: DE RecName: Full=IMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_00139}; DE EC=3.5.4.10 {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=ATIC {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=IMP synthase {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=Inosinicase {ECO:0000255|HAMAP-Rule:MF_00139}; GN Name=purH {ECO:0000255|HAMAP-Rule:MF_00139}; GN OrderedLocusNames=YPO3728, y0502, YP_3091; OS Yersinia pestis. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=632; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO-92 / Biovar Orientalis; RX PubMed=11586360; DOI=10.1038/35097083; RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T., RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., RA Stevens K., Whitehead S., Barrell B.G.; RT "Genome sequence of Yersinia pestis, the causative agent of plague."; RL Nature 413:523-527(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIM10+ / Biovar Mediaevalis; RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002; RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.; RT "Genome sequence of Yersinia pestis KIM."; RL J. Bacteriol. 184:4601-4611(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=91001 / Biovar Mediaevalis; RX PubMed=15368893; DOI=10.1093/dnares/11.3.179; RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., RA Wang J., Huang P., Yang R.; RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate RT avirulent to humans."; RL DNA Res. 11:179-197(2004). CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D- CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467, CC ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.1.2.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino- CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): CC step 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal CC region. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000255|HAMAP- CC Rule:MF_00139}. CC -!- SEQUENCE CAUTION: CC Sequence=AAM84091.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAS63261.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AL590842; CAL22315.1; -; Genomic_DNA. DR EMBL; AE009952; AAM84091.1; ALT_INIT; Genomic_DNA. DR EMBL; AE017042; AAS63261.1; ALT_INIT; Genomic_DNA. DR PIR; AH0453; AH0453. DR RefSeq; WP_002210692.1; NZ_WUCM01000097.1. DR RefSeq; YP_002348608.1; NC_003143.1. DR AlphaFoldDB; Q8ZAR3; -. DR SMR; Q8ZAR3; -. DR IntAct; Q8ZAR3; 4. DR STRING; 214092.YPO3728; -. DR PaxDb; 214092-YPO3728; -. DR DNASU; 1145449; -. DR EnsemblBacteria; AAS63261; AAS63261; YP_3091. DR GeneID; 57974989; -. DR KEGG; ype:YPO3728; -. DR KEGG; ypk:y0502; -. DR KEGG; ypm:YP_3091; -. DR PATRIC; fig|214092.21.peg.4246; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_6; -. DR OMA; IKHNNPC; -. DR OrthoDB; 9802065at2; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000815; Chromosome. DR Proteomes; UP000001019; Chromosome. DR Proteomes; UP000002490; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IBA:GO_Central. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central. DR CDD; cd01421; IMPCH; 1. DR Gene3D; 3.40.140.20; -; 2. DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1. DR HAMAP; MF_00139; PurH; 1. DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR036914; MGS-like_dom_sf. DR InterPro; IPR002695; PurH-like. DR NCBIfam; TIGR00355; purH; 1. DR PANTHER; PTHR11692:SF0; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC; 1. DR PANTHER; PTHR11692; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH; 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. DR SUPFAM; SSF53927; Cytidine deaminase-like; 1. DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1. DR PROSITE; PS51855; MGS; 1. PE 3: Inferred from homology; KW Hydrolase; Multifunctional enzyme; Purine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1..529 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_0000192154" FT DOMAIN 1..148 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" SQ SEQUENCE 529 AA; 57154 MW; 5A76A59B82F39BFE CRC64; MQQRRPIRRA LLSVSDKAGI IEFAQALSQR GIELLSTGGT ARLLADAGLP VTEVSDYTGF PEMMDGRVKT LHPKVHGGIL GRRGQDDGIM AQHGIQPIDI VVVNLYPFAQ TVARPDCSLE DAVENIDIGG PTMVRSAAKN HKDVAIVVKS SDYPAIITEL DNNDGSLTYP TRFNLAIKAF EHTAAYDSMI ANYFGTLVPP YHGDTEQPSG HFPRTLNLNY IKKQDMRYGE NSHQQAAFYI EEDVKEASVA TAQQLQGKAL SYNNIADTDA ALECVKEFSE PACVIVKHAN PCGVAIGDSI LAAYERAYQT DPTSAFGGII AFNRELDAAT ASAIISRQFV EVIIAPTVSS DALALLAAKQ NVRVLTCGQW QARSAGLDFK RVNGGLLVQE RDLGMVTAAD LRVVSKRQPT EQELRDALFC WKVAKFVKSN AIVYARDNMT IGIGAGQMSR VYSAKIAGIK AADEGLEVAG SAMASDAFFP FRDGIDAAAA VGITCVIQPG GSIRDDEVIA AADEHSIAMI FTDMRHFRH //