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Database: UniProt
Entry: F8AJI0_PYRYC
LinkDB: F8AJI0_PYRYC
Original site: F8AJI0_PYRYC 
ID   F8AJI0_PYRYC            Unreviewed;       438 AA.
AC   F8AJI0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   16-JAN-2019, entry version 50.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000256|HAMAP-Rule:MF_00138};
GN   OrderedLocusNames=PYCH_16060 {ECO:0000313|EMBL:AEH25272.1};
OS   Pyrococcus yayanosii (strain CH1 / JCM 16557).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=529709 {ECO:0000313|EMBL:AEH25272.1, ECO:0000313|Proteomes:UP000008386};
RN   [1] {ECO:0000313|EMBL:AEH25272.1, ECO:0000313|Proteomes:UP000008386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH1 / JCM 16557 {ECO:0000313|Proteomes:UP000008386};
RX   PubMed=21705594; DOI=10.1128/JB.05345-11;
RA   Jun X., Lupeng L., Minjuan X., Oger P., Fengping W., Jebbar M.,
RA   Xiang X.;
RT   "Complete genome sequence of the obligate piezophilic
RT   hyperthermophilic archaeon Pyrococcus yayanosii CH1.";
RL   J. Bacteriol. 193:4297-4298(2011).
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         Evidence={ECO:0000256|HAMAP-Rule:MF_00138};
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. {ECO:0000256|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00138}.
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DR   EMBL; CP002779; AEH25272.1; -; Genomic_DNA.
DR   RefSeq; WP_013906328.1; NC_015680.1.
DR   STRING; 529709.PYCH_16060; -.
DR   EnsemblBacteria; AEH25272; AEH25272; PYCH_16060.
DR   GeneID; 10838175; -.
DR   KEGG; pya:PYCH_16060; -.
DR   eggNOG; arCOG04415; Archaea.
DR   eggNOG; COG0151; LUCA.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; 58022at2157; -.
DR   BioCyc; PYAY529709:G1GYE-1593-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000008386; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.90.600.10; -; 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; IPR011054; Rudment_hybrid_motif.
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   TIGRFAMs; TIGR00877; purD; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00184; GARS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008386};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:AEH25272.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138}.
FT   DOMAIN      108    316       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   COILED      243    263       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   438 AA;  47885 MW;  5265AC6FC3FCDF2F CRC64;
     MKVLLVGGGG REHAIGEALA RAGAELYVVS KHKNPGLARL AKDYSLAKET DVPKVVGYAE
     RLSVELAFIG PEAPLEAGIV NALEEAGIPT VGPTKEAARL ETNKAFARAF MEKHKIPGRK
     LFRVFDDIGE MRAWIDEFGK PVVVKPLGLT GGKGVKVVGY QLKDNEEAKA YAEELIRKDG
     KVLIEERTDG VEFTFQVFTD GKHVVPMPLA QDYPHAYEGD EGPITGGMGS YSCANHLLPF
     VTREDYERAL ETLKATVEAM RKEGTPYKGI LYGQFMLSRD GPVIIEYNAR FGDPEAMNVL
     PLLKTSLLEI AEGIVDGNLK GAEFERKATV VKYIAPKGYP TSPVKGVRIE LDEKAIAETG
     ARLYYASVDE NLILLGSRAL AVVGIADTLE EAERIAQAAI GYVKGKIFYR RDVGTKESVE
     KRVRILIELG KDFKPLAC
//
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