PUR2_DICDI
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 03-AUG-2022, entry version 112.
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 (Slime mold).
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;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-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}.
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DR EMBL; AAFI02000153; EAL62377.1; -; Genomic_DNA.
DR RefSeq; XP_635881.1; XM_630789.1.
DR AlphaFoldDB; Q54GJ2; -.
DR SMR; Q54GJ2; -.
DR STRING; 44689.DDB0230084; -.
DR PaxDb; Q54GJ2; -.
DR PRIDE; Q54GJ2; -.
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; 3.30.1330.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.90.600.10; -; 1.
DR Gene3D; 3.90.650.10; -; 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 PANTHER; PTHR10520; PTHR10520; 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; SM01210; GARS_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00877; purD; 1.
DR TIGRFAMs; TIGR00878; purM; 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
