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Database: UniProt
Entry: H9UES3_FERPD
LinkDB: H9UES3_FERPD
Original site: H9UES3_FERPD 
ID   H9UES3_FERPD            Unreviewed;       413 AA.
AC   H9UES3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=phosphoribosylamine--glycine ligase {ECO:0000256|ARBA:ARBA00013255};
DE            EC=6.3.4.13 {ECO:0000256|ARBA:ARBA00013255};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|ARBA:ARBA00042242};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|ARBA:ARBA00042864};
GN   OrderedLocusNames=Ferpe_1968 {ECO:0000313|EMBL:AFG36016.1};
OS   Fervidobacterium pennivorans (strain DSM 9078 / Ven5).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=771875 {ECO:0000313|EMBL:AFG36016.1, ECO:0000313|Proteomes:UP000007384};
RN   [1] {ECO:0000313|Proteomes:UP000007384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9078 / Ven5 {ECO:0000313|Proteomes:UP000007384};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Noll K.M., Woyke T.;
RT   "Complete sequence of Fervidobacterium pennivorans DSM 9078.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the GARS family.
CC       {ECO:0000256|ARBA:ARBA00038345}.
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DR   EMBL; CP003260; AFG36016.1; -; Genomic_DNA.
DR   RefSeq; WP_014452443.1; NC_017095.1.
DR   AlphaFoldDB; H9UES3; -.
DR   STRING; 771875.Ferpe_1968; -.
DR   KEGG; fpe:Ferpe_1968; -.
DR   PATRIC; fig|771875.3.peg.1995; -.
DR   eggNOG; COG0151; Bacteria.
DR   HOGENOM; CLU_027420_3_0_0; -.
DR   OrthoDB; 9807240at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000007384; 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-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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   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:0000313|EMBL:AFG36016.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT   DOMAIN          105..309
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   413 AA;  45325 MW;  BF2D92E21E55C213 CRC64;
     MSGVRKVKRV LVLGSGGREH AIGWAFKNAG CEVSFYPGNA GTKLEGKNLN ISEAELLSGN
     ILGEFDLVIP GSEDFLVKGI ADGRINVFGP DSAGARLEGS KCFAKLFMEK YNIPTARFQI
     ARNKVQLVDA LKSFTPPYVI KADGLAQGKG VIIEDNFSNA VENGSKLMDG TLIPGVSGPV
     VVDEFLKGWE LSAIAIVSGR KFALLPFTRD YKRVFTGNKG PNTGGMGAYG PVEINQKLVE
     KIRTIFDKTL FGLEKEGIYY KGFLYIGLMI VDEEPYVLEY NVRLGDPETE VIVAMEPEKF
     VGNVLKAFNN EDFEEYKSSK FAVDVVVASE GYPESPRKGQ KIVIENIENS EKEGNILFYA
     GVKEQNGELV VSGGRVLHSV GIDNELGKAR EKAYKNIQNI HFEGMFYRDD IAL
//
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