ID   PUR2_BACSU              Reviewed;         422 AA.
AC   P12039;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   27-MAR-2024, entry version 153.
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};
GN   OrderedLocusNames=BSU06530;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3036807; DOI=10.1016/s0021-9258(18)47560-6;
RA   Ebbole D.J., Zalkin H.;
RT   "Cloning and characterization of a 12-gene cluster from Bacillus subtilis
RT   encoding nine enzymes for de novo purine nucleotide synthesis.";
RL   J. Biol. Chem. 262:8274-8287(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969499; DOI=10.1099/13500872-142-11-3027;
RA   Borriss R., Porwollik S., Schroeter R.;
RT   "The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a
RT   region devoted to purine uptake and metabolism, and containing the genes
RT   cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide
RT   sequence.";
RL   Microbiology 142:3027-3031(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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; J02732; AAA22684.1; -; Genomic_DNA.
DR   EMBL; AF011544; AAB72186.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12473.1; -; Genomic_DNA.
DR   PIR; B29183; AJBSAG.
DR   RefSeq; NP_388535.1; NC_000964.3.
DR   RefSeq; WP_003242993.1; NZ_JNCM01000032.1.
DR   PDB; 2XCL; X-ray; 2.10 A; A=1-422.
DR   PDB; 2XD4; X-ray; 2.65 A; A=1-422.
DR   PDBsum; 2XCL; -.
DR   PDBsum; 2XD4; -.
DR   AlphaFoldDB; P12039; -.
DR   SMR; P12039; -.
DR   STRING; 224308.BSU06530; -.
DR   PaxDb; 224308-BSU06530; -.
DR   EnsemblBacteria; CAB12473; CAB12473; BSU_06530.
DR   GeneID; 938741; -.
DR   KEGG; bsu:BSU06530; -.
DR   PATRIC; fig|224308.179.peg.709; -.
DR   eggNOG; COG0151; Bacteria.
DR   InParanoid; P12039; -.
DR   OrthoDB; 9807240at2; -.
DR   PhylomeDB; P12039; -.
DR   BioCyc; BSUB:BSU06530-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000001570; 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; 3.40.50.20; -; 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   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..422
FT                   /note="Phosphoribosylamine--glycine ligase"
FT                   /id="PRO_0000151436"
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..7
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           10..19
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          26..32
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   TURN            38..40
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           51..60
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          63..68
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           71..75
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           78..84
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   TURN            94..97
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           98..101
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           103..112
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          120..124
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           126..136
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          138..146
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          153..158
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           159..170
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           176..179
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          180..186
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          190..200
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          203..206
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          210..217
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           218..220
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          221..233
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           239..248
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           250..259
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          265..275
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          278..287
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   TURN            290..292
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           293..296
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           297..299
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           304..312
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          325..333
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   TURN            334..337
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          345..347
FT                   /evidence="ECO:0007829|PDB:2XD4"
FT   STRAND          353..365
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          367..372
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   STRAND          374..386
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           387..401
FT                   /evidence="ECO:0007829|PDB:2XCL"
FT   HELIX           414..420
FT                   /evidence="ECO:0007829|PDB:2XCL"
SQ   SEQUENCE   422 AA;  45280 MW;  4EF390A85CC90FB2 CRC64;
     MNVLIIGKGG REHTLAWKAA QSSLVENVFA APGNDGMAAS AQLVNIEESD HAGLVSFAKQ
     NQVGLTIVGP EVPLIEGLVD EFEKAGLHVF GPSKAAAIIE GSKQFAKDLM KKYDIPTAEY
     ETFTSFDEAK AYVQEKGAPI VIKADGLAAG KGVTVAMTEE EAIACLHDFL EDEKFGDASA
     SVVIEEYLSG EEFSLMAFVK GEKVYPMVIA QDHKRAFDGD KGPNTGGMGA YSPVPQISEE
     TVRHAVETIV KPAAKAMVQE GRSFTGVLYA GLMLTENGSK VIEFNARFGD PETQVVLPRM
     ESDLVQVLLD LLDDKEVDLR WKDTAAVSVV LASEGYPESY AKGTPIGSLA AETEQVVVFH
     AGTKAEGGEF VTNGGRVANV TAFDETFEAA RDRVYKAVDE IFKPGLFFRK DIGARALKAA
     QK
//