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Database: UniProt
Entry: A0A150LD12_9BACI
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ID   A0A150LD12_9BACI        Unreviewed;       418 AA.
AC   A0A150LD12;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-FEB-2019, entry version 17.
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=B4102_0139 {ECO:0000313|EMBL:KYD10233.1};
OS   Bacillus sporothermodurans.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD10233.1, ECO:0000313|Proteomes:UP000075666};
RN   [1] {ECO:0000313|EMBL:KYD10233.1, ECO:0000313|Proteomes:UP000075666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4102 {ECO:0000313|EMBL:KYD10233.1,
RC   ECO:0000313|Proteomes:UP000075666};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A.,
RA   Holsappel S., Eijlander R.T., Kuipers O.P.;
RT   "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated
RT   from Foods.";
RL   Submitted (JAN-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KYD10233.1}.
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DR   EMBL; LQYN01000015; KYD10233.1; -; Genomic_DNA.
DR   RefSeq; WP_066227684.1; NZ_LQYN01000015.1.
DR   EnsemblBacteria; KYD10233; KYD10233; B4102_0139.
DR   PATRIC; fig|46224.3.peg.1159; -.
DR   BioCyc; GCF_001587375:B4102_RS03710-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000075666; 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:UP000075666};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:KYD10233.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075666}.
FT   DOMAIN      107    313       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   418 AA;  45420 MW;  7D451766E058E94A CRC64;
     MNVLVIGRGG REHAICKKVK ESSLVENVYC APGNAGIRKD AVIVPISEMN FSDLIAFAKD
     NEIDLTIVGP EDPLSAGIVN EFKQAGLNVF GPTKEAALIE GSKSFAKDLM KKYLIPTSAY
     ETFEQYDEAK KYIQEHGAPV VIKADGLAAG KGVIVALTEE EALEGLEELM VDQKFGTAST
     KVVIEEFLLG EEFSLMAFVN GEAVYPMVIA QDHKRAFDGD KGPNTGGMGA YSPVPQIPQQ
     EVERAVQEIL IPTVNALKAE GRSFCGILYA GLILTNEGPK VIEFNARFGD PETQVVLSRL
     ESDLVQVILD LQNETTPTLS WSNDCSVGVV LASNGYPSTY EKGIEIPNLN KFESSTLVFH
     AGTERNEENA IVSNGGRVLL IAAKGNDLKD AVKKVYVEMD KIKSDRFFYR SDIGLKAL
//
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