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Database: UniProt
Entry: A0A0A2EYI7_9PORP
LinkDB: A0A0A2EYI7_9PORP
Original site: A0A0A2EYI7_9PORP 
ID   A0A0A2EYI7_9PORP        Unreviewed;       414 AA.
AC   A0A0A2EYI7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   10-APR-2019, entry version 22.
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   ORFNames=HW49_00985 {ECO:0000313|EMBL:KGN82772.1};
OS   Porphyromonadaceae bacterium COT-184 OH4590.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; unclassified Porphyromonadaceae.
OX   NCBI_TaxID=1517682 {ECO:0000313|EMBL:KGN82772.1, ECO:0000313|Proteomes:UP000030107};
RN   [1] {ECO:0000313|EMBL:KGN82772.1, ECO:0000313|Proteomes:UP000030107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-184 OH4590 {ECO:0000313|Proteomes:UP000030107};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA   Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S.,
RA   Eisen J.A.;
RT   "Porphyromonadaceae COT-184_OH4590 Genome sequencing.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KGN82772.1}.
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DR   EMBL; JRAN01000006; KGN82772.1; -; Genomic_DNA.
DR   RefSeq; WP_036825929.1; NZ_JRAN01000006.1.
DR   STRING; 1517682.HW49_00985; -.
DR   EnsemblBacteria; KGN82772; KGN82772; HW49_00985.
DR   OrthoDB; 932854at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000030107; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000030107};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:KGN82772.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030107}.
FT   DOMAIN      107    311       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   414 AA;  45019 MW;  CC829324D4ED920E CRC64;
     MKVLVIGGGG REHAICAALK KSKKVDKIYC ASGNAGIASI AECVSIGDTD IEALAAFAKS
     RTIDLTVVGP EASLAAGIVD RFEDEGLKIF GASRRATQIE SSKEFAKNLM RKYDIPTAKY
     AIFADYNEAI AYLERHQAPI VIKYDGLAAG KGVVVAMTDN EARNALKDML LDHKYGDAKV
     IMEEFMQGPE FSFMCFVGGE NVYPMALAQD HKRAFDNDQG PNTGGMGAYS PLPFITYEDR
     AFALEGIMKK TAKALVAEGC PFYGVLYGGL MKTAGGIKVI EFNARFGDPE TEVVLPLLKS
     DIFEVFNDVI DGRTPVLEWD TRAAIGFVLA SKGYPESYDK GIEIKGLDSL QGVEVYHMGT
     KSDGNRLLTN GGRVLFVTAL ADTLSDARKH AITQISKIEC KNLFYRRDIG YQAV
//
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