PUR2_ZYMMO
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 03-AUG-2022, entry version 118.
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}; OrderedLocusNames=ZMO0299;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; 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 PRIDE; Q9FDL5; -.
DR EnsemblBacteria; AAV88923; AAV88923; ZMO0299.
DR GeneID; 58026161; -.
DR KEGG; zmo:ZMO0299; -.
DR eggNOG; COG0151; Bacteria.
DR HOGENOM; CLU_027420_3_1_5; -.
DR OrthoDB; 932854at2; -.
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 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.
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
