ID A0A061P216_9BACL Unreviewed; 413 AA.
AC A0A061P216;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=JCM19038_2682 {ECO:0000313|EMBL:GAK08882.1};
OS Geomicrobium sp. JCM 19038.
OC Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX NCBI_TaxID=1460635 {ECO:0000313|EMBL:GAK08882.1, ECO:0000313|Proteomes:UP000027014};
RN [1] {ECO:0000313|EMBL:GAK08882.1, ECO:0000313|Proteomes:UP000027014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19038 {ECO:0000313|EMBL:GAK08882.1,
RC ECO:0000313|Proteomes:UP000027014};
RA Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA Hongoh Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL Genome Announc. 2:e00622-14(2014).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAK08882.1}.
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DR EMBL; BAXA01000009; GAK08882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061P216; -.
DR eggNOG; COG0151; Bacteria.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000027014; Unassembled WGS sequence.
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; 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 {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}; Reference proteome {ECO:0000313|Proteomes:UP000027014}.
FT DOMAIN 108..313
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 413 AA; 43941 MW; A9C3CA6EC9BBD522 CRC64;
MMNVLVVGNG GREHVLAWKL AQSKRVETVY VAPGNPGMED VATCLDVDIA NHDELIQNAK
ELNVELTVIG PEAPLAAGVV DAFTEAGLAV FGPSKKAALI EGSKAFAKDL MKQYNIPTAN
YEVFTDFEEA LHYTKTQGAP IVVKADGLAA GKGVTVAVTL DEAELALRDI LLDDAFGTGA
KVVLEEYLEG EELSILALVN GDTVVPLAES QDHKRAFDAD QGPNTGGMGA YSPVPHIDRS
DISKAIETIV KPTAQAMIKE GTPFTGVLYA GLMMTAEGPK TIEFNARFGD PEAQVVLSRM
ESDLVDVIQA VLNDEEPAVH WLEEAVVGVV LAADGYPSSY MKGLPVPKRT SGEVFYAGVE
RGSKGLTSSG GRVYIAMGKG SSLKEAQANA YENVDSLDTS GYHYRTDIAY RAL
//
