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Database: UniProt
Entry: Q9FDL5
LinkDB: Q9FDL5
Original site: Q9FDL5 
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   16-JAN-2019, entry version 103.
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; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; 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.,
RA   Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M.,
RA   Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y.,
RA   Kang H.L., Lee S.Y., Lee K.J., 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-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: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;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-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; Positions=86, 99, 123; Evidence={ECO:0000305};
CC       Sequence=AAV88923.2; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AF212041; AAG02154.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE008692; AAV88923.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_012817395.1; NZ_CP023715.1.
DR   ProteinModelPortal; Q9FDL5; -.
DR   SMR; Q9FDL5; -.
DR   EnsemblBacteria; AAV88923; AAV88923; ZMO0299.
DR   KEGG; zmo:ZMO0299; -.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   OrthoDB; 932854at2; -.
DR   BioCyc; ZMOB264203:G1FZK-260-MONOMER; -.
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; 3.30.1490.20; -; 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; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    417       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151507.
FT   DOMAIN      107    312       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     133    193       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       282    282       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       284    284       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   CONFLICT    235    235       R -> S (in Ref. 1; AAG02154).
FT                                {ECO:0000305}.
FT   CONFLICT    395    395       D -> Y (in Ref. 1; AAG02154).
FT                                {ECO:0000305}.
FT   CONFLICT    405    405       D -> V (in Ref. 1; AAG02154).
FT                                {ECO:0000305}.
FT   CONFLICT    413    413       G -> E (in Ref. 1; AAG02154).
FT                                {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
//
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