ID   PUR9_SALTY              Reviewed;         529 AA.
AC   P26978; Q9L9H7;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   27-MAR-2024, entry version 138.
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=STM4176; ORFNames=STMF1.30;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-529.
RX   PubMed=1954258; DOI=10.1016/0167-4781(91)90202-w;
RA   Chopra A.K., Peterson J.W., Prasad R.;
RT   "Nucleotide sequence analysis of purH and purD genes from Salmonella
RT   typhimurium.";
RL   Biochim. Biophys. Acta 1090:351-354(1991).
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, ECO:0000305}.
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DR   EMBL; AF170176; AAF33520.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL23004.1; -; Genomic_DNA.
DR   EMBL; M66160; AAA27197.1; -; Genomic_DNA.
DR   PIR; S18488; DTEBPH.
DR   RefSeq; NP_463045.1; NC_003197.2.
DR   RefSeq; WP_001187509.1; NC_003197.2.
DR   AlphaFoldDB; P26978; -.
DR   SMR; P26978; -.
DR   STRING; 99287.STM4176; -.
DR   PaxDb; 99287-STM4176; -.
DR   GeneID; 1255702; -.
DR   KEGG; stm:STM4176; -.
DR   PATRIC; fig|99287.12.peg.4390; -.
DR   HOGENOM; CLU_016316_5_2_6; -.
DR   OMA; IKHNNPC; -.
DR   PhylomeDB; P26978; -.
DR   BioCyc; SENT99287:STM4176-MONOMER; -.
DR   UniPathway; UPA00074; UER00133.
DR   UniPathway; UPA00074; UER00135.
DR   Proteomes; UP000001014; 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_0000192120"
FT   DOMAIN          1..148
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT   CONFLICT        302..303
FT                   /note="DA -> EP (in Ref. 2; AAA27197)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        399
FT                   /note="A -> R (in Ref. 2; AAA27197)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        418
FT                   /note="L -> W (in Ref. 2; AAA27197)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        494
FT                   /note="S -> T (in Ref. 2; AAA27197)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   529 AA;  57467 MW;  5D713504AD644778 CRC64;
     MQQRRPVRRA LLSVSDKAGI IEFAQALSAR GVELLSTGGT ARLLAEKGLP VTEVSDYTGF
     PEMMDGRVKT LHPKVHGGIL GRRGQDDAIM EQHHIAPIDM VVVNLYPFAE TVAREGCSLE
     DAVENIDIGG PTMVRSAAKN HKDVAIVVKS SDYDAIIKEM DANEGSLTLD TRFDLAIKAF
     EHTAAYDSMI ANYFGSMVPA YHGESKEAAG RFPRTLNLNF IKKQDMRYGE NSHQQAAFYI
     EENVKEASVA TAQQVQGKAL SYNNIADTDA ALECVKEFNE PACVIVKHAN PCGVAVSTTI
     LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSATE EALKITAAKQ
     NVRVLTCGQW AQRVPGLDFK RVNGGLLVQD RDLGMVSEAE LRVVSKRQPT EQELRDALFC
     WKVAKFVKSN AIVYAKENMT IGIGAGQMSR VYSAKIAGIK AADEGLEVKG SAMASDAFFP
     FRDGIDAAAA VGVSCVIQPG GSIRDDEVIA AADEHGIAMI FTDMRHFRH
//