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Database: UniProt
Entry: E4RL69_HALHG
LinkDB: E4RL69_HALHG
Original site: E4RL69_HALHG 
ID   E4RL69_HALHG            Unreviewed;       430 AA.
AC   E4RL69;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
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   OrderedLocusNames=Halsa_2346 {ECO:0000313|EMBL:ADQ15750.1};
OS   Halanaerobium hydrogeniformans (Halanaerobium sp. (strain sapolanicus)).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=656519 {ECO:0000313|EMBL:ADQ15750.1, ECO:0000313|Proteomes:UP000007434};
RN   [1] {ECO:0000313|EMBL:ADQ15750.1, ECO:0000313|Proteomes:UP000007434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Begemann M.B., Mormile M.R., Wall J.D., Elias D.A., Woyke T.;
RT   "Complete sequence of Halanaerobium sp. sapolanicus.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ15750.1, ECO:0000313|Proteomes:UP000007434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RX   PubMed=21602336; DOI=10.1128/JB.05209-11;
RA   Brown S.D., Begemann M.B., Mormile M.R., Wall J.D., Han C.S., Goodwin L.A.,
RA   Pitluck S., Land M.L., Hauser L.J., Elias D.A.;
RT   "Complete Genome Sequence of the Haloalkaliphilic, Hydrogen Producing
RT   Halanaerobium hydrogenoformans.";
RL   J. Bacteriol. 193:3682-3683(2011).
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}.
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DR   EMBL; CP002304; ADQ15750.1; -; Genomic_DNA.
DR   RefSeq; WP_013406809.1; NC_014654.1.
DR   AlphaFoldDB; E4RL69; -.
DR   STRING; 656519.Halsa_2346; -.
DR   KEGG; has:Halsa_2346; -.
DR   eggNOG; COG0151; Bacteria.
DR   HOGENOM; CLU_027420_3_1_9; -.
DR   OrthoDB; 9807240at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000007434; 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; 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:UP000007434}.
FT   DOMAIN          107..313
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   430 AA;  47299 MW;  1B957B6ADFA7632B CRC64;
     MKVLVVGNGG REHALAWKLF RSERVDEIFV APGNDGMTDI AQTVDIKADD IEGLANFARE
     NEIGMTVVGP EEPLVAGIVD YFVEESLPIF GPKKQAALLE GSKVFAKDIL NKYNIPTAEY
     EVFTDPDSAL NYLKNADYPL VIKAEGLAQG KGSIVASNFQ DSQDAVTRIM EDKTFGDAGD
     RIVVEDFLEG EELSVFALTD GQTILPITTA RDHKAVFEGD EGPNTGGMGA YSPAVNTDEE
     LMDKICREIL RPTLHALNSE GIDYRGVLHI GMILTESGPA VIDYNARFGD PETQVILPRL
     GEDIIELMEM TNNVELKYKK EIKVSGSVAV CVVLASAGYP LTFNTGYEIK GLDNLKHHDD
     LLIFHAGTKI VEDKYYTDGG RVLGLTVVDN GLLNTINKVY QYIEEVEFED MHYRTDIGFS
     ISEIAEKELN
//
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