ID D3E0Y9_METRM Unreviewed; 458 AA.
AC D3E0Y9;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 ECO:0000313|EMBL:ADC47963.1};
GN OrderedLocusNames=mru_2113 {ECO:0000313|EMBL:ADC47963.1};
OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 /
OS OCM 146 / M1) (Methanobacterium ruminantium).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=634498 {ECO:0000313|EMBL:ADC47963.1, ECO:0000313|Proteomes:UP000008680};
RN [1] {ECO:0000313|EMBL:ADC47963.1, ECO:0000313|Proteomes:UP000008680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1
RC {ECO:0000313|Proteomes:UP000008680};
RX PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA Janssen P.H., Dey D., Attwood G.T.;
RT "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium
RT reveals new possibilities for controlling ruminant methane emissions.";
RL PLoS ONE 5:E8926-E8926(2010).
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; CP001719; ADC47963.1; -; Genomic_DNA.
DR AlphaFoldDB; D3E0Y9; -.
DR STRING; 634498.mru_2113; -.
DR KEGG; mru:mru_2113; -.
DR PATRIC; fig|634498.28.peg.2115; -.
DR eggNOG; arCOG04415; Archaea.
DR HOGENOM; CLU_027420_3_0_2; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000008680; 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:UP000008680}.
FT DOMAIN 127..339
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 458 AA; 49903 MW; 07025916E9B53229 CRC64;
MIFSKLENNQ LLKKLLNGEI KMKVLVVGTG AREHAICDAL KDDVDLYAYM SKNNPGISKI
STFKKGDEGE VDEVAKFAKE NEIELAVIGP EAPLGKGIVN ALEAVGVPCV GPAQESARIE
TDKSFMRNLF EKYQIKGSLT YKVFDNYEDI SAFLDTYEKD VVVKPVGLTG GKGVKIVGDH
LKDNQDAKAY AKEVMDNAMG GFAQVIIEEK VVGEEFTIQA FCDGENLAAM PAAQDHPHAF
ENDQGLITGG MGSYSDVGGL LPFLTQEDYD EAVDIMKETL KAIAKETTPY KGILYGQFML
SKDGPKLIEY NARFGDPEAM NVLPLLKTPM VDVCKAIVDG KLEDVEFEDK ASVCKYIVPD
GYPDTPHAGE LIEIDEEAIE ALGAKVFYAA VSQEDDGVHL SGSRALGIVA QGDTIAEAEK
IAEEACGLVE GNVYHRRDVG TEALIQKRID HMEAIRNE
//
