ID   PUR9_DEIRA              Reviewed;         510 AA.
AC   Q9RW01;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 2.
DT   27-MAR-2024, entry version 125.
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=DR_0868;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS   27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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=AAF10444.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000513; AAF10444.1; ALT_INIT; Genomic_DNA.
DR   PIR; B75467; B75467.
DR   RefSeq; NP_294592.1; NC_001263.1.
DR   RefSeq; WP_027479694.1; NZ_JMLF01000010.1.
DR   AlphaFoldDB; Q9RW01; -.
DR   SMR; Q9RW01; -.
DR   STRING; 243230.DR_0868; -.
DR   PaxDb; 243230-DR_0868; -.
DR   EnsemblBacteria; AAF10444; AAF10444; DR_0868.
DR   GeneID; 69517114; -.
DR   KEGG; dra:DR_0868; -.
DR   PATRIC; fig|243230.17.peg.1052; -.
DR   eggNOG; COG0138; Bacteria.
DR   HOGENOM; CLU_016316_5_2_0; -.
DR   InParanoid; Q9RW01; -.
DR   OrthoDB; 9802065at2; -.
DR   UniPathway; UPA00074; UER00133.
DR   UniPathway; UPA00074; UER00135.
DR   Proteomes; UP000002524; Chromosome I.
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..510
FT                   /note="Bifunctional purine biosynthesis protein PurH"
FT                   /id="PRO_0000192090"
FT   DOMAIN          1..143
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ   SEQUENCE   510 AA;  54046 MW;  668734C53416269C CRC64;
     MTKRALISVS DKTGVVEFAA QLQQRGWELL STGGTFATLS GAGIPVRQVS DVTGFPEMLD
     GRVKTLHPAI HGGILARREA GHLGQLAAQD IGTIDLVCVN LYPFRETVAR GAPDPEVIEN
     IDIGGPAMIR SAAKNHDAVL VLVDPADYAL ALQDEVSPAE RRRLAAKAYR HTSEYDAAIT
     AYLSGESDEL PTQLPEHLSL DLTRTAQVRY GENPHQPGAI YRWGNARGPV IDAQVVAGKP
     MSFNNYADAD AAWSLCQELA AQEQGAVCVA VKHANPCGVA VAADVKTAWE RARDADTLSV
     FGGVVAVSQP VDFGAAQSMK GTFLEVLIAP DVTPDAVEWF AAKKPDLRVL IAGQPQGVSV
     LDVRPLTGGF AVQERDARPW DDLCPEVVTE RQPSEQEWAD LRFAWAVVKG ARSNAVALCK
     GGVTVGLGAG AVSRIWAAER AIANAGEAAQ GAVLASEAFF PFDDVVRLAA SAGVTAVLQP
     GGAKRDPEVI AACNELGISM VFTGSRHFRH
//