ID   PUR9_BACCN              Reviewed;         511 AA.
AC   A7GKI2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 92.
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}; OrderedLocusNames=Bcer98_0277;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-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:57454,
CC         ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; 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}.
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DR   EMBL; CP000764; ABS20640.1; -; Genomic_DNA.
DR   RefSeq; WP_011983399.1; NC_009674.1.
DR   AlphaFoldDB; A7GKI2; -.
DR   SMR; A7GKI2; -.
DR   STRING; 315749.Bcer98_0277; -.
DR   EnsemblBacteria; ABS20640; ABS20640; Bcer98_0277.
DR   GeneID; 56415834; -.
DR   KEGG; bcy:Bcer98_0277; -.
DR   eggNOG; COG0138; Bacteria.
DR   HOGENOM; CLU_016316_5_2_9; -.
DR   OMA; WRVAKFV; -.
DR   OrthoDB; 1049662at2; -.
DR   UniPathway; UPA00074; UER00133.
DR   UniPathway; UPA00074; UER00135.
DR   Proteomes; UP000002300; 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   Gene3D; 3.40.140.20; -; 2.
DR   Gene3D; 3.40.50.1380; -; 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   PANTHER; PTHR11692; PTHR11692; 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; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR00355; purH; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Multifunctional enzyme; Purine biosynthesis; Transferase.
FT   CHAIN           1..511
FT                   /note="Bifunctional purine biosynthesis protein PurH"
FT                   /id="PRO_1000076473"
FT   DOMAIN          1..145
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ   SEQUENCE   511 AA;  55681 MW;  6670148C002D0444 CRC64;
     MKKRALVSVS NKTGVVEFVK GLLEQGIEVI STGGTKKLLE ENGLQVMGIS EVTGFPEIMD
     GRVKTLHPNI HGGLLAVRDN EAHVAEMSEL GIQLIDFVVV NLYPFKETIA KPDVTFADAI
     ENIDIGGPTM IRSAAKNHKF VSVIVDPADY DVVLAELKEK GEVTDETKRK LAAKVFRHTA
     AYDALISNYL TEQMGEESPE ILTVTFEKKQ DLRYGENPHQ KATFYKAPFA VASSVAYAEQ
     LHGKELSYNN INDADAALSI VKEFTEPAVV AVKHMNPCGV GVGTDIHEAY TRAYEADPVS
     IFGGIIAANR EIDKRVAEKL HEIFLEIIIA PSFSKEALEV LQSKKNLRLL TVNIEKTTSA
     SKKLTSVQGG LLVQEEDTLA LNEETIIIPT KREPTEQEWN DLKLAWKVVK HVKSNAIVLA
     KDNMTIGVGA GQMNRVGSAK IAISQAGSKA QGSALASDAF FPMPDTVEEA AKAGITAIIQ
     PGGSIRDEDS IKKADEYGIT MVFTGVRHFK H