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Database: UniProt
Entry: A0A0D6ML10_9PROT
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ID   A0A0D6ML10_9PROT        Unreviewed;       420 AA.
AC   A0A0D6ML10;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 21.
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=Tasa_017_049 {ECO:0000313|EMBL:GAN54166.1};
OS   Tanticharoenia sakaeratensis NBRC 103193.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Tanticharoenia.
OX   NCBI_TaxID=1231623 {ECO:0000313|EMBL:GAN54166.1, ECO:0000313|Proteomes:UP000032679};
RN   [1] {ECO:0000313|EMBL:GAN54166.1, ECO:0000313|Proteomes:UP000032679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103193 {ECO:0000313|EMBL:GAN54166.1,
RC   ECO:0000313|Proteomes:UP000032679};
RA   Azuma Y., Hadano H., Hirakawa H., Matsushita K.;
RT   "Genome sequencing of Tanticharoenia sakaeratensis NBRC 103193.";
RL   Submitted (OCT-2012) 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:GAN54166.1}.
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DR   EMBL; BALE01000017; GAN54166.1; -; Genomic_DNA.
DR   RefSeq; WP_048848710.1; NZ_BALE01000017.1.
DR   EnsemblBacteria; GAN54166; GAN54166; Tasa_017_049.
DR   OrthoDB; 932854at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000032679; 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:UP000032679};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:GAN54166.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032679}.
FT   DOMAIN      107    313       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   420 AA;  42583 MW;  D67558B891381A2E CRC64;
     MRVLLVGSGG REHALAASLA RSPDLSALFI APGNPGMAAL GTLVPIPVTD IAGLATFAKD
     NAIDLVVPGP EAPLVAGLAD ACAEIGIPCA GPSRAAAQLE GSKTFTKEVC DAAGIPTARW
     ERFTDAGAAQ TFVQRRGAPI VIKADGLAAG KGVVVAQTVA EAEAAIDMML TDGSFGDAGA
     SVVIEECLMG PEISLFAFCA GTDCTLIGAA RDHKRLGDGD TGPNTGGMGA ISPPPGFDRA
     AQEHALDILV RPMLAEMAKR GTPFRGVIFA GAMLTDEGPK LIEYNVRFGD PEAETLLPRL
     TSDLLPALRD LAADTLGASP VTFSDDASIS IILAARGYPD APIKGGPISG IAEAEAVPGV
     RVFHAGTALD ANGTLVAAGG RVLAVSATAP DAATARARAY EAAGRIVWSD AVYRRDIGGL
//
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