ID   PUR92_YEAST             Reviewed;         592 AA.
AC   P38009; D6VZU3;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   10-JUN-2026, entry version 214.
DE   RecName: Full=Bifunctional purine biosynthesis protein ADE17;
DE   Includes:
DE     RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase;
DE              EC=2.1.2.3 {ECO:0000269|PubMed:10877846, ECO:0000305|PubMed:9143321, ECO:0000305|PubMed:9169872};
DE     AltName: Full=5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase {ECO:0000303|PubMed:9143321};
DE     AltName: Full=AICAR transformylase {ECO:0000303|PubMed:9143321};
DE   Includes:
DE     RecName: Full=Inosine 5'-monophosphate cyclohydrolase {ECO:0000305};
DE              Short=IMP cyclohydrolase {ECO:0000303|PubMed:9143321};
DE              EC=3.5.4.10 {ECO:0000269|PubMed:10877846, ECO:0000305|PubMed:9169872};
DE     AltName: Full=ATIC {ECO:0000303|PubMed:10877846};
DE     AltName: Full=IMP synthase;
DE     AltName: Full=Inosinicase;
GN   Name=ADE17 {ECO:0000303|PubMed:9143321}; OrderedLocusNames=YMR120C;
GN   ORFNames=YM8564.02C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872; DOI=10.1038/387s090;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   PROTEIN SEQUENCE OF 140-150 AND 389-400.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7895733; DOI=10.1002/elps.11501501210;
RA   Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA   Volpe T., Warner J.R., McLaughlin C.S.;
RT   "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL   Electrophoresis 15:1466-1486(1994).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX   PubMed=9143321; DOI=10.1006/abbi.1997.9919;
RA   Tibbetts A.S., Appling D.R.;
RT   "Saccharomyces cerevisiae expresses two genes encoding isozymes of 5-
RT   aminoimidazole-4-carboxamide ribonucleotide transformylase.";
RL   Arch. Biochem. Biophys. 340:195-200(1997).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP   SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10877846; DOI=10.1074/jbc.m909851199;
RA   Tibbetts A.S., Appling D.R.;
RT   "Characterization of two 5-aminoimidazole-4-carboxamide ribonucleotide
RT   transformylase/inosine monophosphate cyclohydrolase isozymes from
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 275:20920-20927(2000).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the last two steps of
CC       purine biosynthesis (PubMed:10877846, PubMed:9143321). Acts as a
CC       transformylase that incorporates a formyl group to the AMP analog AICAR
CC       (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to
CC       produce the intermediate formyl-AICAR (FAICAR) (PubMed:10877846,
CC       PubMed:9143321). Also catalyzes the cyclization of FAICAR to IMP
CC       (PubMed:10877846, PubMed:9143321). {ECO:0000269|PubMed:10877846,
CC       ECO:0000269|PubMed:9143321}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D-
CC         ribosyl)imidazole-4-carboxamide + (6S)-5,6,7,8-tetrahydrofolate;
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:0000269|PubMed:10877846, ECO:0000305|PubMed:9143321,
CC         ECO:0000305|PubMed:9169872};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=IMP + H2O = 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:0000269|PubMed:10877846, ECO:0000305|PubMed:9169872};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=22 uM for
CC         5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with
CC         (6S)-10-formyltetrahydrofolate as cosubstrate) (at pH 7.4)
CC         {ECO:0000269|PubMed:10877846};
CC         KM=63 uM for (6S)-10-formyltetrahydrofolate (with
CC         5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide as
CC         cosubstrate) (at pH 7.4) {ECO:0000269|PubMed:10877846};
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:0000269|PubMed:10877846, ECO:0000269|PubMed:9143321}.
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:0000269|PubMed:10877846, ECO:0000269|PubMed:9143321}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10877846}.
CC   -!- INTERACTION:
CC       P38009; P54113: ADE16; NbExp=6; IntAct=EBI-14223, EBI-14213;
CC       P38009; P50278: SOL1; NbExp=2; IntAct=EBI-14223, EBI-17675;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10877846}.
CC   -!- INDUCTION: Repressed by adenine (PubMed:10877846). Not induced during
CC       growth on the non-fermentable carbon source glycerol with ethanol
CC       (PubMed:10877846). {ECO:0000269|PubMed:10877846}.
CC   -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC       region. {ECO:0000250|UniProtKB:P31939}.
CC   -!- DISRUPTION PHENOTYPE: Simultaneous knockout of ADE16 leads to adenine
CC       and histidine auxotrophy. {ECO:0000269|PubMed:10877846,
CC       ECO:0000269|PubMed:9143321}.
CC   -!- MISCELLANEOUS: Present with 60900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}.
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DR   EMBL; Z49273; CAA89269.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10017.1; -; Genomic_DNA.
DR   PIR; S54489; S54489.
DR   RefSeq; NP_013839.1; NM_001182621.1.
DR   AlphaFoldDB; P38009; -.
DR   SMR; P38009; -.
DR   BioGRID; 35297; 131.
DR   DIP; DIP-6288N; -.
DR   FunCoup; P38009; 1220.
DR   IntAct; P38009; 48.
DR   MINT; P38009; -.
DR   STRING; 4932.YMR120C; -.
DR   iPTMnet; P38009; -.
DR   PaxDb; 4932-YMR120C; -.
DR   PeptideAtlas; P38009; -.
DR   EnsemblFungi; YMR120C_mRNA; YMR120C; YMR120C.
DR   GeneID; 855149; -.
DR   KEGG; sce:YMR120C; -.
DR   AGR; SGD:S000004727; -.
DR   SGD; S000004727; ADE17.
DR   VEuPathDB; FungiDB:YMR120C; -.
DR   eggNOG; KOG2555; Eukaryota.
DR   HOGENOM; CLU_016316_3_2_1; -.
DR   InParanoid; P38009; -.
DR   OMA; IKHNNPC; -.
DR   OrthoDB; 6017153at2759; -.
DR   BioCyc; MetaCyc:YMR120C-MONOMER; -.
DR   BioCyc; YEAST:YMR120C-MONOMER; -.
DR   Reactome; R-SCE-73817; Purine ribonucleoside monophosphate biosynthesis.
DR   UniPathway; UPA00074; UER00133.
DR   UniPathway; UPA00074; UER00135.
DR   BioGRID-ORCS; 855149; 4 hits in 10 CRISPR screens.
DR   CD-CODE; E03F929F; Stress granule.
DR   PRO; PR:P38009; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P38009; protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IDA:SGD.
DR   GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IDA:SGD.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IDA:SGD.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IDA:SGD.
DR   CDD; cd01421; IMPCH; 1.
DR   FunFam; 3.40.140.20:FF:000003; Bifunctional purine biosynthesis protein; 1.
DR   FunFam; 3.40.50.1380:FF:000003; Bifunctional purine biosynthesis protein; 1.
DR   FunFam; 1.10.287.440:FF:000001; Bifunctional purine biosynthesis protein PURH; 1.
DR   Gene3D; 1.10.287.440; -; 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; IPR024050; AICAR_Tfase_insert_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; NF005492; PRK07106.1; 1.
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   Cytoplasm; Direct protein sequencing; Hydrolase; Multifunctional enzyme;
KW   Purine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..592
FT                   /note="Bifunctional purine biosynthesis protein ADE17"
FT                   /id="PRO_0000192160"
FT   DOMAIN          1..147
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT   ACT_SITE        138
FT                   /note="Proton donor/acceptor; for FAICAR cyclization
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   ACT_SITE        267
FT                   /note="Proton acceptor; for AICAR formyltransferase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         35..38
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         65..68
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         102..103
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         126..127
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         206..207
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         267
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         315
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         338
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         430
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         450
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         451
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P31335"
FT   BINDING         541
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         546
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P31335"
FT   BINDING         565..566
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P31335"
FT   BINDING         588
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   SITE            266
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   CONFLICT        389
FT                   /note="R -> A (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   592 AA;  65263 MW;  8ABA71761B512242 CRC64;
     MANYTKTAIL SVYDKTGLLD LARGLIEKNV RILASGGTAR MIRDAGFPIE DVSAITHAPE
     MLGGRVKTLH PAVHGGILAR DIDSDEKDLK EQHIEKVDYV VCNLYPFKET VAKVGVTIPE
     AVEEIDIGGV TLLRAAAKNH ARVTILSDPK DYSEFLSELS SNGEISQDLR NRLALKAFEH
     TADYDAAISD FFRKQYSEGQ AQITLRYGAN PHQKPAQAYV SQQDSLPFKV LCGSPGYINL
     LDALNSWPLV KELSASLNLP AAASFKHVSP AGAAVGIPLS DVEKQVYFVA DIENLSPLAC
     AYARARGADR MSSFGDWIAL SNIVDVPTAK IISREVSDGV IAPGYEPEAL AILSKKKGGK
     YCILQIDPNY VPEAVERRQV YGVTLEQKRN DAIINQSTFK EIVSQNKNLT EQAIIDLTVA
     TIAIKYTQSN SVCYARNGMV VGLGAGQQSR IHCTRLAGDK ADNWWFRQHP RVLEIKWAKG
     VKRPEKSNAI DLFVTGQIPT EEPELSEYQS KFEEIPKPFT PEERKEWLSK LTNVSLSSDA
     FFPFPDNVYR AVKSGVKYIA APSGSVMDKV VFSAADSFDL VYVENPIRLF HH
//