ID   PUR9_SCHPO              Reviewed;         585 AA.
AC   O74928; P78892;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Bifunctional purine biosynthesis protein ade10;
DE   Includes:
DE     RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase;
DE              EC=2.1.2.3 {ECO:0000250|UniProtKB:P54113};
DE     AltName: Full=5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase;
DE     AltName: Full=AICAR transformylase;
DE   Includes:
DE     RecName: Full=Inosine 5'-monophosphate cyclohydrolase {ECO:0000305};
DE              Short=IMP cyclohydrolase {ECO:0000305};
DE              EC=3.5.4.10 {ECO:0000250|UniProtKB:P54113};
DE     AltName: Full=ATIC;
DE     AltName: Full=IMP synthase;
DE     AltName: Full=Inosinicase;
GN   Name=ade10; ORFNames=SPCPB16A4.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=9802209;
RX   DOI=10.1002/(sici)1097-0061(1998100)14:14<1307::aid-yea308>3.0.co;2-4;
RA   Liedtke C., Schmidt H.;
RT   "Molecular cloning and sequence analysis of the Schizosaccharomyces pombe
RT   ade10+ gene.";
RL   Yeast 14:1307-1310(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-585.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the last two steps of
CC       purine biosynthesis. Acts as a transformylase that incorporates a
CC       formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-
CC       ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-
CC       AICAR (FAICAR). Also catalyzes the cyclization of FAICAR to IMP.
CC       {ECO:0000250|UniProtKB:P54113}.
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:0000250|UniProtKB:P54113};
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:0000250|UniProtKB:P54113};
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.
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.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P54113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P54113}.
CC   -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC       region. {ECO:0000250|UniProtKB:P31939}.
CC   -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}.
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DR   EMBL; Y16419; CAA76207.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAC39322.1; -; Genomic_DNA.
DR   EMBL; D89243; BAA13904.1; -; mRNA.
DR   PIR; T43150; T43150.
DR   RefSeq; NP_588027.1; NM_001023018.2.
DR   AlphaFoldDB; O74928; -.
DR   SMR; O74928; -.
DR   BioGRID; 276129; 15.
DR   STRING; 284812.O74928; -.
DR   iPTMnet; O74928; -.
DR   MaxQB; O74928; -.
DR   PaxDb; 4896-SPCPB16A4-03c-1; -.
DR   EnsemblFungi; SPCPB16A4.03c.1; SPCPB16A4.03c.1:pep; SPCPB16A4.03c.
DR   GeneID; 2539569; -.
DR   KEGG; spo:SPCPB16A4.03c; -.
DR   PomBase; SPCPB16A4.03c; ade10.
DR   VEuPathDB; FungiDB:SPCPB16A4.03c; -.
DR   eggNOG; KOG2555; Eukaryota.
DR   HOGENOM; CLU_016316_3_2_1; -.
DR   InParanoid; O74928; -.
DR   OMA; IKHNNPC; -.
DR   PhylomeDB; O74928; -.
DR   Reactome; R-SPO-73817; Purine ribonucleoside monophosphate biosynthesis.
DR   UniPathway; UPA00074; UER00133.
DR   UniPathway; UPA00074; UER00135.
DR   PRO; PR:O74928; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IDA:PomBase.
DR   GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IDA:PomBase.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IMP:PomBase.
DR   GO; GO:0006188; P:IMP biosynthetic process; IMP:PomBase.
DR   CDD; cd01421; IMPCH; 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; 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   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Multifunctional enzyme; Purine biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..585
FT                   /note="Bifunctional purine biosynthesis protein ade10"
FT                   /id="PRO_0000192158"
FT   DOMAIN          1..142
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT   ACT_SITE        133
FT                   /note="Proton donor/acceptor; for FAICAR cyclization
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   ACT_SITE        260
FT                   /note="Proton acceptor; for AICAR formyltransferase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         30..33
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         60..63
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         97..98
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         121..122
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   BINDING         200..201
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         260
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         308
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         331
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         423
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         443
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         444
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P31335"
FT   BINDING         534
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         539
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P31335"
FT   BINDING         558..559
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250|UniProtKB:P31335"
FT   BINDING         581
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            259
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P31939"
FT   CONFLICT        404
FT                   /note="K -> Q (in Ref. 3; BAA13904)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   585 AA;  64123 MW;  103031D3F957529F CRC64;
     MYALLSVYDK TGLLELAKAL TSKGVKLLGS GGTAKMIRES GMEVADVSSI TNAPEILGGR
     VKTLHPAVHG GILARDIPSD EKDLVEQSIE KIDIVVCNLY PFRETIAKPN VTIPEAVEEI
     DIGGVTLLRA AAKNHARVTI LSDPADYATF TDKFLSDKLT QDDRNTYALK AFASTASYDA
     AITDYFRKQY AAGVDQLTLR YGANPHQSPA QAFMEQGPLP FKVLCGSPGY INLMDALNSW
     PLVKELRENI GIPAAASFKH VSPAGAAVGL PLSDVEKKVY FVSDITEFTP LACAYARARG
     ADRMSSFGDF IALSDTVDVC TARIISREVS DGVIAPGYEP EALELLKKKK GGKYCVLQMD
     PKYVPAEIET RQVYGISLQQ HRNHAKIDFS LFEKVVSKNK DLPKSALIDL VIATTALKYT
     QSNSVCYAKN GMVVGLGAGQ QSRIHCNRLA GDKADNWWLR HHPKVLGMQF KKSAKRPEKS
     NAIDLYVLDA VPAEGSEREQ WESAFETIPE PLTKKEREEF LATCKDVVCA SDAFFPFPDN
     IYRLAQSGVK YVAAPGGSVM DQAVRDTANE FNMVFSEIPL RLFHH
//