PUR2_AQUAE
ID PUR2_AQUAE Reviewed; 424 AA.
AC O66949;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000255|HAMAP-Rule:MF_00138};
DE EC=6.3.4.13 {ECO:0000255|HAMAP-Rule:MF_00138};
DE AltName: Full=GARS {ECO:0000255|HAMAP-Rule:MF_00138};
DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_00138};
DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000255|HAMAP-Rule:MF_00138};
GN Name=purD {ECO:0000255|HAMAP-Rule:MF_00138}; OrderedLocusNames=aq_742;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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:0000255|HAMAP-Rule:MF_00138};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
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:0000255|HAMAP-Rule:MF_00138}.
CC -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP-
CC Rule:MF_00138}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000657; AAC06907.1; -; Genomic_DNA.
DR PIR; B70365; B70365.
DR RefSeq; NP_213510.1; NC_000918.1.
DR RefSeq; WP_010880448.1; NC_000918.1.
DR PDB; 2YW2; X-ray; 1.80 A; A/B=1-424.
DR PDB; 2YYA; X-ray; 2.40 A; A/B=1-424.
DR PDBsum; 2YW2; -.
DR PDBsum; 2YYA; -.
DR AlphaFoldDB; O66949; -.
DR SMR; O66949; -.
DR STRING; 224324.aq_742; -.
DR EnsemblBacteria; AAC06907; AAC06907; aq_742.
DR KEGG; aae:aq_742; -.
DR PATRIC; fig|224324.8.peg.593; -.
DR eggNOG; COG0151; Bacteria.
DR HOGENOM; CLU_027420_3_1_0; -.
DR InParanoid; O66949; -.
DR OMA; KATVCKY; -.
DR OrthoDB; 932854at2; -.
DR BRENDA; 6.3.4.13; 396.
DR UniPathway; UPA00074; UER00125.
DR EvolutionaryTrace; O66949; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.30.1490.20; -; 1.
DR Gene3D; 3.90.600.10; -; 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 PANTHER; PTHR43472; PTHR43472; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR SMART; SM01210; GARS_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR00877; purD; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..424
FT /note="Phosphoribosylamine--glycine ligase"
FT /id="PRO_0000151434"
FT DOMAIN 107..313
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT BINDING 133..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2YW2"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 190..200
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:2YW2"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 265..275
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 278..287
FT /evidence="ECO:0007829|PDB:2YW2"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 293..298
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 323..332
FT /evidence="ECO:0007829|PDB:2YW2"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 358..368
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:2YW2"
FT STRAND 376..388
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 389..400
FT /evidence="ECO:0007829|PDB:2YW2"
FT TURN 414..418
FT /evidence="ECO:0007829|PDB:2YW2"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:2YW2"
SQ SEQUENCE 424 AA; 47430 MW; 06EB10D23A68E2FD CRC64;
MKVLVVGNGG REHAIAWKVA QSPLVKELYV AKGNAGIWEI AKRVDISPTD VEKLAEFAKN
EGVDFTIVGP EAPLVEGIVD EFEKRGLKIF GPNKEAAKLE GSKAFAKTFM KKYGIPTARY
EVFTDFEKAK EYVEKVGAPI VVKADGLAAG KGAVVCETVE KAIETLDRFL NKKIFGKSSE
RVVIEEFLEG EEASYIVMIN GDRYVPLPTS QDHKRLLDED KGPNTGGMGA YSPTPVINEE
VEKRIREEIV ERVIKGLKEE GIYYRGFLYA GLMITKEGPK VLEFNVRLGD PEAQPILMRV
KNDFLETLLN FYEGKDVHIK EDERYALDVV LASRGYPEKP ETGKIIHGLD YLKSMEDVVV
FHAGTKKEGN FTVTSGGRVL NVCAYGKTLK EAKERAYEAI RYVCFEGMHY RKDIGDKAFK
YLSE
