ID   PUR2_DICDI              Reviewed;         815 AA.
AC   Q54GJ2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 118.
DE   RecName: Full=Bifunctional purine biosynthetic protein purD;
DE   Includes:
DE     RecName: Full=Phosphoribosylamine--glycine ligase;
DE              EC=6.3.4.13 {ECO:0000250|UniProtKB:P20772};
DE     AltName: Full=Glycinamide ribonucleotide synthetase;
DE              Short=GAR synthetase {ECO:0000250|UniProtKB:P20772};
DE              Short=GARS;
DE     AltName: Full=Phosphoribosylglycinamide synthetase;
DE   Includes:
DE     RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE              EC=6.3.3.1 {ECO:0000250|UniProtKB:P20772};
DE     AltName: Full=AIR synthase;
DE              Short=AIR synthetase {ECO:0000250|UniProtKB:P20772};
DE              Short=AIRS;
DE     AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
GN   Name=purD {ECO:0000312|dictyBase:DDB_G0290121};
GN   ORFNames=DDB_G0290121 {ECO:0000312|dictyBase:DDB_G0290121};
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 515-533 AND 667-682, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=AX2;
RA   Bienvenut W.V., Ura S., Insall R.H.;
RL   Submitted (JUL-2009) to UniProtKB.
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:0000250|UniProtKB:P20772}.
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:0000250|UniProtKB:P20772};
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:0000250|UniProtKB:P20772};
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 no magnesium or manganese ion 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
CC       {ECO:0000250|UniProtKB:P20772}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000153; EAL62377.1; -; Genomic_DNA.
DR   RefSeq; XP_635881.1; XM_630789.1.
DR   AlphaFoldDB; Q54GJ2; -.
DR   SMR; Q54GJ2; -.
DR   STRING; 44689.Q54GJ2; -.
DR   PaxDb; 44689-DDB0230084; -.
DR   EnsemblProtists; EAL62377; EAL62377; DDB_G0290121.
DR   GeneID; 8627491; -.
DR   KEGG; ddi:DDB_G0290121; -.
DR   dictyBase; DDB_G0290121; purD.
DR   eggNOG; KOG0237; Eukaryota.
DR   HOGENOM; CLU_005361_1_0_1; -.
DR   InParanoid; Q54GJ2; -.
DR   OMA; EVMQACC; -.
DR   PhylomeDB; Q54GJ2; -.
DR   Reactome; R-DDI-73817; Purine ribonucleoside monophosphate biosynthesis.
DR   UniPathway; UPA00074; UER00125.
DR   UniPathway; UPA00074; UER00129.
DR   PRO; PR:Q54GJ2; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IBA:GO_Central.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central.
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; 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.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Ligase; Magnesium;
KW   Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome.
FT   CHAIN           1..815
FT                   /note="Bifunctional purine biosynthetic protein purD"
FT                   /id="PRO_0000328326"
FT   DOMAIN          113..343
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   REGION          6..452
FT                   /note="GARS"
FT                   /evidence="ECO:0000255"
FT   REGION          469..801
FT                   /note="AIRS"
FT                   /evidence="ECO:0000255"
FT   BINDING         139..200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ   SEQUENCE   815 AA;  87706 MW;  C24A183386A06FC6 CRC64;
     MTIKNNILVI GSGSREHAIT WKLLESNQVD KVILVPGNAS SSTMERVITV ECSKIDAESI
     SNICKEHNVE YVFVGPEVPL VDGIVDGLKR KGISCFGPTK KAAQLEGSKV FCKDFMARNN
     IPSARYQTFT DYNKAKQYIE SLNYKIVLKA SGCAAGKGVL IPNNKEEELE GLKRIMVDKE
     FGSAGDEIVI EEFLDGEECS LMCFSDGYSL VVMPPAQDHK RIFDGDKGAN TGGMGAYAPA
     PFIVDCNNNA TTDKSKSKSS FGTIIDRCVE TILKPTINGM RKEGKPFVGV LFAGLMVSSS
     SSTTNDKVIN VLEFNCRMGD PETQVVLPLL ETDLFEIVLA CIEGRLDGLD VKWSNKFAVT
     VVAASKGYPD SYPKGLKING LLENKNTNDN IIFQAGTTVN GSNDIVTNGG RVLSCTSVSE
     SLEDAIKNSY KLIETISFEG MQYRKDIGQK ALNHLERKKQ QQANSKQSVS YSESGVDIER
     GDAVVDNIGP LAKATTRLGC VSDLGGFGAL FDTKAAGFRD PILVSGTDGV GTKLKIAQEL
     GIHDSIGIDL VAMCVNDVVV QGAEPLFFLD YFATGRIHVD VATQVVSGIA RGCKESGCAL
     IGGETAEMPG MYKDGEYDLA GFSVGAVERD QMLPSNIQEG NILLGLASSG VHSNGYSLVR
     YLIETKSGGL TYNSIAPFDS SKTLGQVLLT PTKLYVLSCL AAIKSGGVNG LAHITGGGIT
     ENLPRVIPDG LDCEVELGSW EILPIFKYLV ELGNMETEEL LKTFNSGIGM ILIVSPDKVD
     SITKSLESNN EKVYKIGKII NSKTSKQSKS KVIYK
//