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Database: UniProt
Entry: A0A125S2M3_9FLAO
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Original site: A0A125S2M3_9FLAO 
ID   A0A125S2M3_9FLAO        Unreviewed;       424 AA.
AC   A0A125S2M3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|ARBA:ARBA00013255, ECO:0000256|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000256|ARBA:ARBA00013255, ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|ARBA:ARBA00042242, ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|ARBA:ARBA00042864, ECO:0000256|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000256|HAMAP-Rule:MF_00138};
GN   ORFNames=AXF12_02345 {ECO:0000313|EMBL:AMD84467.1};
OS   Capnocytophaga haemolytica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=45243 {ECO:0000313|EMBL:AMD84467.1, ECO:0000313|Proteomes:UP000065822};
RN   [1] {ECO:0000313|Proteomes:UP000065822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 32990 {ECO:0000313|Proteomes:UP000065822};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00138};
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:0000256|ARBA:ARBA00005174,
CC       ECO:0000256|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|ARBA:ARBA00038345,
CC       ECO:0000256|HAMAP-Rule:MF_00138}.
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DR   EMBL; CP014227; AMD84467.1; -; Genomic_DNA.
DR   RefSeq; WP_066428033.1; NZ_LT906449.1.
DR   AlphaFoldDB; A0A125S2M3; -.
DR   STRING; 45243.AXF12_02345; -.
DR   KEGG; chg:AXF12_02345; -.
DR   OrthoDB; 9807240at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000065822; Chromosome.
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; 3.40.50.20; -; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00138};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00138}.
FT   DOMAIN          112..323
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   424 AA;  47137 MW;  A027BDE64098921A CRC64;
     MNILILGSGG REHAFAYKVV QSPHCERLYV APGNGGTAAI ATNVDISTTD FQAVKRLVIE
     KDIKMVIVGP EDPLVHGIYD FFKRDTYLAE NVQIIAPSQE GAKLEGSKEF AKQFMQRHSI
     PTAKYNSFTK DRLEEGYRFL ETLKPPYVLK ADGLAAGKGV LILPSIDEAR TALHDMLIEA
     KFGEASHKIV IEEFLDGIEL SCFVLTDGKH YKILPTAKDY KRVGEGDTGL NTGGMGAISP
     VPFVDDLFMQ KIEERIIKPT ILGLQQEHID YKGFIFIGLI KVGEDPFVIE YNVRMGDPET
     EVILPRIESD LVNIFKALEK QELDKMTLKI TPKTAATVML TSGGYPETYQ KGFPITGLKD
     VNESLVFHAG TAIKDGKTVT TGGRVLAVTS LANDFHKALA QSYKNIEKIH FERQYFRRDI
     GFDL
//
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