ID   PUR2_ZYMMO              Reviewed;         417 AA.
AC   Q9FDL5; Q5NQT1;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000255|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000255|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000255|HAMAP-Rule:MF_00138};
GN   OrderedLocusNames=ZMO0299;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Lee H.J., Kang H.S.;
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
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:0000255|HAMAP-Rule:MF_00138};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
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:0000255|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00138}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG02154.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAV88923.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF212041; AAG02154.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE008692; AAV88923.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_012817395.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q9FDL5; -.
DR   SMR; Q9FDL5; -.
DR   STRING; 264203.ZMO0299; -.
DR   GeneID; 79904483; -.
DR   KEGG; zmo:ZMO0299; -.
DR   eggNOG; COG0151; Bacteria.
DR   HOGENOM; CLU_027420_3_1_5; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000001173; Chromosome.
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; 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; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 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   NCBIfam; TIGR00877; purD; 1.
DR   PANTHER; PTHR43472; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE; 1.
DR   PANTHER; PTHR43472:SF1; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 1.
DR   SMART; SM01209; GARS_A; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00184; GARS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..417
FT                   /note="Phosphoribosylamine--glycine ligase"
FT                   /id="PRO_0000151507"
FT   DOMAIN          107..312
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT   REGION          206..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         133..193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT   BINDING         284
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT   CONFLICT        235
FT                   /note="R -> S (in Ref. 1; AAG02154)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="D -> Y (in Ref. 1; AAG02154)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        405
FT                   /note="D -> V (in Ref. 1; AAG02154)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        413
FT                   /note="G -> E (in Ref. 1; AAG02154)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   417 AA;  44044 MW;  C31176955B0D9FC2 CRC64;
     MNVLLIGTGG REHALAWKIA QSPSLDTFYA TTGNPGIAKL AKPADITVTD HAAVVRFCQD
     NAIDLVVIGP EAPLVDGLGN SLRAASIAVF GPDKAAAQLE GSKGFTKDLC ARYNIPTARY
     QRCRSAEEAK AALDNFSTPV VIKADGLAGG KGVIIAESRL EAEQAIQDMT AGAFGKAGLE
     IVVEEFMQGE EASFFAISDG ETVRPFGTAR DHKRVGDGDT GPNTGGMGAY SPATRLTADL
     EKRVMQEIVT PTVQAMKEQG MPFVGILYAG LMLTSEGPKL IEYNARLGDP ECQVLMMRLE
     SDILPLLYAA ATGKLQAQPE PTFSKDYAVT VVIAAQGYPA SPKKGGIITR LNEAEANGAV
     VFQAGTTLDN QTLKANGGRV LNVTAKAADF NAARDLAYQA VNVIDYPDGF WRGDIGL
//