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Database: UniProt
Entry: Q99148
LinkDB: Q99148
Original site: Q99148 
ID   PUR2_YARLI              Reviewed;         788 AA.
AC   Q99148;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JAN-2019, entry version 123.
DE   RecName: Full=Bifunctional purine biosynthetic protein ADE1;
DE   Includes:
DE     RecName: Full=Phosphoribosylamine--glycine ligase;
DE              EC=6.3.4.13;
DE     AltName: Full=Glycinamide ribonucleotide synthetase;
DE              Short=GARS;
DE     AltName: Full=Phosphoribosylglycinamide synthetase;
DE   Includes:
DE     RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE              EC=6.3.3.1;
DE     AltName: Full=AIR synthase;
DE              Short=AIRS;
DE     AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
GN   Name=ADE1; OrderedLocusNames=YALI0F21010g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
OS   lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Strick C.A., James L.C., Cole K.E., Elsenboss L.A.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58089,
CC         ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(formamido)-N(1)-(5-phospho-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:58478,
CC         ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 2/2.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 2/2.
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}.
DR   EMBL; U40565; AAA85393.1; -; Genomic_DNA.
DR   EMBL; CR382132; CAG78498.1; -; Genomic_DNA.
DR   RefSeq; XP_505689.1; XM_505689.1.
DR   ProteinModelPortal; Q99148; -.
DR   SMR; Q99148; -.
DR   STRING; 4952.XP_505689.1; -.
DR   PRIDE; Q99148; -.
DR   EnsemblFungi; CAG78498; CAG78498; YALI0_F21010g.
DR   GeneID; 2907698; -.
DR   KEGG; yli:YALI0F21010g; -.
DR   HOGENOM; HOG000030315; -.
DR   InParanoid; Q99148; -.
DR   KO; K11788; -.
DR   OMA; LLERHNC; -.
DR   UniPathway; UPA00074; UER00125.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000001300; Chromosome F.
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; 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   PANTHER; PTHR10520; PTHR10520; 2.
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.
DR   PROSITE; PS00184; GARS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    788       Bifunctional purine biosynthetic protein
FT                                ADE1.
FT                                /FTId=PRO_0000074940.
FT   DOMAIN      114    323       ATP-grasp.
FT   NP_BIND     140    201       ATP. {ECO:0000250}.
FT   REGION        1    432       GARS.
FT   REGION      442    752       AIRS.
FT   METAL       291    291       Manganese. {ECO:0000250}.
FT   METAL       293    293       Manganese. {ECO:0000250}.
SQ   SEQUENCE   788 AA;  83759 MW;  6EC170ECB27AFCF4 CRC64;
     MSLRILLVGN GGREHALAWK LAQSPLVERI FVAPGNGGTD NPQGKIENIA IGSSQKDFAK
     LVEFAQSKDV GLVIPGPEQP LVEGIETHFR KVGIPVFGPS EKAAVMEGSK TFSKDFMKKH
     NIPTAAFENF TDYNKAVDYV KKVGHRVVIK ASGLAAGKGV LIPTSTEEAI AAVKEVMQDK
     AFGEAGDEVV IEEFLEGDEL SILAFSDGYT VVDMPPAQDH KRIGDGDQGL NTGGMGAYCP
     APIGTPALLQ EIKESILQPT IDGMRRDGIP FVGMLFTGIM LTPDGKPKVL EYNVRFGDPE
     TQTILPLLSD DTDLAEVMLA CVERRLDAVT LRVKPDAHAV TVVMSAGGYP ESYKKGDAIT
     VGGLPEQTYI FHAGTASENG QVITAGGRVI ASTAVAPTLK DAVAQAYKGA DAVEFNGKYN
     RKDIAYKAFR DAEKTSGGIT YAQAGVSIDN GNKLVQQIKE KVKSTARPGT DSVIGGFGGL
     FDLKAAGFRD PLLVGATDGV GTKLKIAQSI DKHDTVGIDL VAMNVNDLVV QGAEPLVFLD
     YYATGKLDVN AAAAFVGGVA DGCIQAGCAL IGGETAEMPG IYYGNDYDAN GTSIGAVERD
     AVLPRMDEIA KGDAILGLAS SGVHSNGFSL VRKIIEHAGL TYTDACPWDQ SKSLGEALLT
     PTRIYVKQLL PVINAKLTSA LAHITGGGLV ENIPRILPEN YSAKIDVSTW PLPPVFQWLG
     KAGNVPKEDI SKTLNMGIGM ILVVKQEKVA EVTQLLEKVG EKVYQIGEIV PDNDVDEKTV
     LINTENWY
//
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