ID   PUR2_HELPY              Reviewed;         424 AA.
AC   O25817;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Phosphoribosylamine--glycine ligase;
DE            EC=6.3.4.13;
DE   AltName: Full=GARS;
DE   AltName: Full=Glycinamide ribonucleotide synthetase;
DE   AltName: Full=Phosphoribosylglycinamide synthetase;
GN   Name=purD; OrderedLocusNames=HP_1218;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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   -!- 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.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000305}.
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DR   EMBL; AE000511; AAD08261.1; -; Genomic_DNA.
DR   PIR; B64672; B64672.
DR   RefSeq; NP_208010.1; NC_000915.1.
DR   RefSeq; WP_000654350.1; NC_018939.1.
DR   AlphaFoldDB; O25817; -.
DR   SMR; O25817; -.
DR   DIP; DIP-3667N; -.
DR   IntAct; O25817; 3.
DR   MINT; O25817; -.
DR   STRING; 85962.C694_06295; -.
DR   PaxDb; O25817; -.
DR   EnsemblBacteria; AAD08261; AAD08261; HP_1218.
DR   KEGG; hpy:HP_1218; -.
DR   PATRIC; fig|85962.47.peg.1307; -.
DR   eggNOG; COG0151; Bacteria.
DR   OMA; QADNMPF; -.
DR   PhylomeDB; O25817; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR020562; PRibGlycinamide_synth_N.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   PANTHER; PTHR43472; PTHR43472; 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   TIGRFAMs; TIGR00877; purD; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..424
FT                   /note="Phosphoribosylamine--glycine ligase"
FT                   /id="PRO_0000151453"
FT   DOMAIN          111..312
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         137..189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ   SEQUENCE   424 AA;  47504 MW;  F093B63E7DCCCCC2 CRC64;
     MKDNNNYNVL IVGNKGREYA LAQRLQQDER VNALYFCLGN GGTQDLGENL ECEHYEHIVE
     LALKKQIHLA IISEEEFLVL GLTEMLEKAG ILVFGASKEA AKLEASKSYM KAFVKECGIK
     SASYFETNDL KEALSYIQNA SFPLVIKALN KNTSIVYQEE EAIKILEDAF KQSNEPVIIE
     PFLEGFELSV TALIANDDFI LLPFCQNYKR LLEGDNGVNT GGMGAIAPAN FFSNELEEKI
     KNHIFKPTLE KLQADNTPFK GVLLAEIVII EEKGVLEPYL LDFSVRFKDI ECQTILPLLE
     SSLLDLCLAT AKGELHSLEL VFSKEFVMSV ALVSRNYPTS SSPKQTLYID PVDEKKGHLI
     LGEVEQDNGV FESSGGRVIF AIGRGKSLLE ARNHAYEIAQ KVHFEGMFYR KDIGFKVLDL
     KEYS