ID PUR9_CAMJE Reviewed; 510 AA. AC Q9PNY2; Q0P9U6; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 116. 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=Cj0953c; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). 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 --------------------------------------------------------------------------- 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; AL111168; CAL35073.1; -; Genomic_DNA. DR PIR; H81369; H81369. DR RefSeq; WP_002853339.1; NZ_SZUC01000001.1. DR RefSeq; YP_002344351.1; NC_002163.1. DR PDB; 4EHI; X-ray; 2.28 A; A/B=1-510. DR PDBsum; 4EHI; -. DR AlphaFoldDB; Q9PNY2; -. DR SMR; Q9PNY2; -. DR IntAct; Q9PNY2; 1. DR STRING; 192222.Cj0953c; -. DR PaxDb; 192222-Cj0953c; -. DR EnsemblBacteria; CAL35073; CAL35073; Cj0953c. DR GeneID; 905247; -. DR KEGG; cje:Cj0953c; -. DR PATRIC; fig|192222.6.peg.937; -. DR eggNOG; COG0138; Bacteria. DR HOGENOM; CLU_016316_5_2_7; -. DR OrthoDB; 9802065at2; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000799; Chromosome. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. 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 1: Evidence at protein level; KW 3D-structure; Hydrolase; Multifunctional enzyme; Purine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1..510 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_0000192079" FT DOMAIN 1..142 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" FT STRAND 2..9 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 13..22 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 26..29 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 31..39 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 78..83 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 91..99 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 103..109 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 113..118 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 124..133 FT /evidence="ECO:0007829|PDB:4EHI" FT TURN 134..137 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 147..155 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 161..190 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 196..209 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 218..225 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 226..230 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 240..253 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 261..266 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 269..275 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 279..287 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 291..294 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 298..305 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 307..313 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 319..326 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 328..332 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 346..349 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 356..362 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 365..370 FT /evidence="ECO:0007829|PDB:4EHI" FT TURN 376..381 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 382..384 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 386..388 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 392..407 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 413..417 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 420..425 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 431..444 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 453..455 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 464..471 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 476..479 FT /evidence="ECO:0007829|PDB:4EHI" FT HELIX 486..496 FT /evidence="ECO:0007829|PDB:4EHI" FT STRAND 499..502 FT /evidence="ECO:0007829|PDB:4EHI" SQ SEQUENCE 510 AA; 56402 MW; 56F356F04B3A2092 CRC64; MRALLSVSDK EGIVEFGKEL ENLGFEILST GGTFKLLKEN GIKVIEVSDF TKSPELFEGR VKTLHPKIHG GILHKRSDEN HIKQAKENEI LGIDLVCVNL YPFKKTTIMS DDFDEIIENI DIGGPAMIRS AAKNYKDVMV LCDPLDYEKV IETLKKGQND ENFRLNLMIK AYEHTANYDA YIANYMNERF NGGFGASKFI VGQKVFDTKY GENPHQKGAL YEFDAFFSAN FKALKGEASF NNLTDINAAL NLASSFDKAP AIAIVKHGNP CGFAIKENLV QSYIHALKCD SVSAYGGVVA INGTLDEALA NKINEIYVEV IIAANVDEKA LAVFEGKKRI KIFTQESPFL IRSFDKYDFK HIDGGFVYQN SDEVGEDELK NAKLMSQREA SKEELKDLEI AMKIAAFTKS NNVVYVKNGA MVAIGMGMTS RIDAAKAAIA KAKEMGLDLQ GCVLASEAFF PFRDSIDEAS KVGVKAIVEP GGSIRDDEVV KAADEYGMAL YFTGVRHFLH //