PUR2_THEMA
ID PUR2_THEMA Reviewed; 400 AA.
AC Q9X0X7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
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=TM_1250;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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}.
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DR EMBL; AE000512; AAD36325.1; -; Genomic_DNA.
DR PIR; D72277; D72277.
DR RefSeq; NP_229055.1; NC_000853.1.
DR PDB; 1VKZ; X-ray; 2.30 A; A/B=1-400.
DR PDBsum; 1VKZ; -.
DR AlphaFoldDB; Q9X0X7; -.
DR SMR; Q9X0X7; -.
DR STRING; 243274.THEMA_08085; -.
DR DNASU; 898233; -.
DR EnsemblBacteria; AAD36325; AAD36325; TM_1250.
DR KEGG; tma:TM1250; -.
DR PATRIC; fig|243274.18.peg.1564; -.
DR eggNOG; COG0151; Bacteria.
DR InParanoid; Q9X0X7; -.
DR OMA; KATVCKY; -.
DR UniPathway; UPA00074; UER00125.
DR EvolutionaryTrace; Q9X0X7; -.
DR Proteomes; UP000008183; 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..400
FT /note="Phosphoribosylamine--glycine ligase"
FT /id="PRO_0000151495"
FT DOMAIN 99..303
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT BINDING 125..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 182..192
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1VKZ"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 230..249
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 255..265
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 268..277
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 314..322
FT /evidence="ECO:0007829|PDB:1VKZ"
FT TURN 324..328
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 344..352
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:1VKZ"
FT STRAND 360..372
FT /evidence="ECO:0007829|PDB:1VKZ"
FT HELIX 373..386
FT /evidence="ECO:0007829|PDB:1VKZ"
SQ SEQUENCE 400 AA; 44326 MW; 411CE014DD7DE90F CRC64;
MKAVRVHILG SGGREHAIGW AFAKQGYEVH FYPGNAGTKR DGTNHPYEGE KTLKAIPEED
IVIPGSEEFL VEGVSNWRSN VFGPVKEVAR LEGSKVYAKR FMKKYGIRTA RFEVAETPEE
LREKIKKFSP PYVIKADGLA RGKGVLILDS KEETIEKGSK LIIGELIKGV KGPVVIDEFL
AGNELSAMAV VNGRNFVILP FVRDYKRLMD GDRGPNTGGM GSWGPVEIPS DTIKKIEELF
DKTLWGVEKE GYAYRGFLYL GLMLHDGDPY ILEYNVRLGD PETEVIVTLN PEGFVNAVLE
GYRGGKMEPV EPRGFAVDVV LAARGYPDAP EKGKEITLPE EGLIFFAGVA EKDGKLVTNG
GRVLHCMGTG ETKEEARRKA YELAEKVHFE GKTYRRDIAL
