ID   PUR2_SCHPO              Reviewed;         788 AA.
AC   P20772; Q9UUM5;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=Bifunctional purine biosynthetic protein ADE1;
DE   Includes:
DE     RecName: Full=Phosphoribosylamine--glycine ligase;
DE              EC=6.3.4.13 {ECO:0000269|PubMed:967158};
DE     AltName: Full=Glycinamide ribonucleotide synthetase;
DE              Short=GAR synthetase {ECO:0000303|PubMed:967158};
DE              Short=GARS;
DE     AltName: Full=Phosphoribosylglycinamide synthetase;
DE   Includes:
DE     RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE              EC=6.3.3.1 {ECO:0000269|PubMed:967158};
DE     AltName: Full=AIR synthase;
DE              Short=AIR synthetase {ECO:0000303|PubMed:967158};
DE              Short=AIRS;
DE     AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
GN   Name=ade1 {ECO:0000303|PubMed:3502942};
GN   ORFNames=SPBC405.01 {ECO:0000312|PomBase:SPBC405.01}, SPBC4C3.02c;
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=3502942; DOI=10.1007/bf00368061;
RA   McKenzie R., Schuchert P., Kilbey B.;
RT   "Sequence of the bifunctional ade1 gene in the purine biosynthetic pathway
RT   of the fission yeast Schizosaccharomyces pombe.";
RL   Curr. Genet. 12:591-597(1987).
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   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=967158; DOI=10.1007/bf00582878;
RA   Fluri R., Coddington A., Flury U.;
RT   "The product of the ade1: gene in Schizosaccharomyces pombe: a bifunctional
RT   enzyme catalysing two distinct steps in purine biosynthesis.";
RL   Mol. Gen. Genet. 147:271-282(1976).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Catalyzes the second and fifth step in the 'de novo' purine
CC       biosynthesis pathway; contains phosphoribosylamine--glycine ligase
CC       (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS)
CC       activities. {ECO:0000269|PubMed:967158}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681,
CC         ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC         Evidence={ECO:0000269|PubMed:967158};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC         = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC         ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC         Evidence={ECO:0000269|PubMed:967158};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00409};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00409};
CC       Note=Binds two magnesium or manganese ions per subunit. {ECO:0000305};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 2/2. {ECO:0000305}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC       (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC       diphosphate: step 2/2. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the GARS family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the AIR synthase
CC       family. {ECO:0000305}.
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DR   EMBL; X06601; CAA29820.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA16823.1; -; Genomic_DNA.
DR   PIR; S00652; S00652.
DR   RefSeq; NP_596304.1; NM_001022225.2.
DR   AlphaFoldDB; P20772; -.
DR   SMR; P20772; -.
DR   BioGRID; 277549; 4.
DR   STRING; 284812.P20772; -.
DR   iPTMnet; P20772; -.
DR   MaxQB; P20772; -.
DR   PaxDb; 4896-SPBC405-01-1; -.
DR   EnsemblFungi; SPBC405.01.1; SPBC405.01.1:pep; SPBC405.01.
DR   PomBase; SPBC405.01; ade1.
DR   VEuPathDB; FungiDB:SPBC405.01; -.
DR   eggNOG; KOG0237; Eukaryota.
DR   HOGENOM; CLU_005361_1_0_1; -.
DR   InParanoid; P20772; -.
DR   OMA; EVMQACC; -.
DR   PhylomeDB; P20772; -.
DR   Reactome; R-SPO-73817; Purine ribonucleoside monophosphate biosynthesis.
DR   UniPathway; UPA00074; UER00125.
DR   UniPathway; UPA00074; UER00129.
DR   PRO; PR:P20772; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IDA:PomBase.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IDA:PomBase.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IMP:PomBase.
DR   GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IDA:PomBase.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR   CDD; cd02196; PurM; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR   HAMAP; MF_00741; AIRS; 1.
DR   HAMAP; MF_00138; GARS; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR   InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR   InterPro; IPR020559; PRibGlycinamide_synth_CS.
DR   InterPro; IPR020562; PRibGlycinamide_synth_N.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR016188; PurM-like_N.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR004733; PurM_cligase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   NCBIfam; TIGR00877; purD; 1.
DR   NCBIfam; TIGR00878; purM; 1.
DR   PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR   PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 1.
DR   SMART; SM01209; GARS_A; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00184; GARS; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..788
FT                   /note="Bifunctional purine biosynthetic protein ADE1"
FT                   /id="PRO_0000454642"
FT   DOMAIN          115..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   REGION          1..430
FT                   /note="GARS"
FT                   /evidence="ECO:0000255"
FT   REGION          437..769
FT                   /note="AIRS"
FT                   /evidence="ECO:0000255"
FT   BINDING         141..202
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ   SEQUENCE   788 AA;  85231 MW;  0FDE64EEA5F9095D CRC64;
     MEPIIALLIG NGGREHTIAW KLCESPLISK VYVAPGNGGT ASNGAESKME NVNIGVCDFE
     QLVKFALDKD VNLVIPGPEL PLVEGIEGHF RRVGIPCFGP SALAARMEGS KVFSKDFMHR
     NNIPTAVYKS FSNYDHAKSF LDTCTFDVVI KADGLAAGKG VIIPKTKKEA FEALESIMLN
     EEFGSAGKNV VIEELLEGEE LSILTFSDGY TCRSLPPAQD HKRAFDGDKG PNTGGMGCYA
     PTPVASPKLL ETVQSTIIQP TIDGMRHEGY PLVGILFTGL MLTPSGPRVL EYNVRFGDPE
     TQAVLPLLES DLAEIILACV NHRLDAIDIV ISRKFSCAVV CVAGGYPGPY NKGDIITFDA
     LKDKNTRIFH AGTSIRDGNV VTNGGRVLAV EATGDSVEAA VRLAYEGVKT VHFDKMFYRK
     DIAHHALNPK RKTREILTYE NSGVSVDNGN EFVQRIKDLV KSTRRPGADA DIGGFGGIFD
     LKQAGWNDPL LVSATDGVGS KLLIALSLNK HDTVGIDLVA MNVNDLVVQG AEPLIFLDYF
     ATGSLDLKVS TSFVEGVVKG CKQAGCALVG GETSEMPGLY HDGHYDANGT SVGAVSRDDI
     LPKPESFSKG DILLGLASDG VHSNGYSLVR KIVEYSDLEY TSVCPWDKNV RLGDSLLIPT
     RIYVKPLLHV IRKNIVKGMA HITGGGLVEN VPRMLPSHLN AIIDVDTWEV PEVFKWLKDA
     GNVPISDMAR TFNMGIGMVV AVASEDAEET MKELTSVGET VYRIGQLVDK ESSSERCHLV
     NLNKWETF
//