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Database: UniProt
Entry: G4HNL1_9BACL
LinkDB: G4HNL1_9BACL
Original site: G4HNL1_9BACL 
ID   G4HNL1_9BACL            Unreviewed;       422 AA.
AC   G4HNL1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   31-JUL-2019, entry version 45.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000256|HAMAP-Rule:MF_00138};
GN   ORFNames=PaelaDRAFT_5572 {ECO:0000313|EMBL:EHB50176.1};
OS   Paenibacillus lactis 154.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB50176.1, ECO:0000313|Proteomes:UP000003891};
RN   [1] {ECO:0000313|EMBL:EHB50176.1, ECO:0000313|Proteomes:UP000003891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=154 {ECO:0000313|EMBL:EHB50176.1,
RC   ECO:0000313|Proteomes:UP000003891};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA   Allgaier M., Woyke T.J.;
RT   "The draft genome of Paenibacillus lactis 154.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58089,
CC         ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00138};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00138}.
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DR   EMBL; AGIP01000021; EHB50176.1; -; Genomic_DNA.
DR   RefSeq; WP_007132723.1; NZ_AGIP01000021.1.
DR   STRING; 743719.PaelaDRAFT_5572; -.
DR   EnsemblBacteria; EHB50176; EHB50176; PaelaDRAFT_5572.
DR   PATRIC; fig|743719.3.peg.5677; -.
DR   OrthoDB; 932854at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000003891; Unassembled WGS sequence.
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; 3.30.1490.20; -; 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   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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003891};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:EHB50176.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138}.
FT   DOMAIN      107    314       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION      212    233       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   422 AA;  44567 MW;  9E1E2E48E545EDFF CRC64;
     MDILVIGGGG REHAIVWALA KSPKAGKIYC APGNAGIGQL AECVPIAVSE FDKLTAFAVE
     KQVGLVVVGP DDPLADGIVD AFDSTGIPVF GPRKNAAEIE GSKTFMKDLL HKYGIPTAAY
     AKFDDYEEAL VYLRRQGAPI VVKADGLAAG KGVTVARTLE EAEKALSDIM QSKVFGEAGS
     RVVIEEFLEG QEMSILAFVD GETVKPMSAA QDHKPVYDGD QGPNTGGMGT YSPLPHIDPS
     IIEEAVETII KPTAKAMVAE GRPFRGVLFA GLMITPDGKP KTIEFNARFG DPETQVVLPR
     LQTDLLEVFL ATVNGKLADL ELEWSKDAAV CVILASGGYP ASYPKGIAIS GLEDEQEATI
     VFHAGTSRDA DGTWRTNGGR VLGVVGLGAD IAAARAKAYA RAESIAFEGK HNRTDIALKA
     LV
//
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