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Database: UniProt
Entry: A0A0R1PDW7_9LACO
LinkDB: A0A0R1PDW7_9LACO
Original site: A0A0R1PDW7_9LACO 
ID   A0A0R1PDW7_9LACO        Unreviewed;       418 AA.
AC   A0A0R1PDW7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   16-JAN-2019, entry version 20.
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=FD33_GL001489 {ECO:0000313|EMBL:KRL28788.1};
OS   Lactobacillus paralimentarius DSM 13238 = JCM 10415.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1122151 {ECO:0000313|EMBL:KRL28788.1, ECO:0000313|Proteomes:UP000051908};
RN   [1] {ECO:0000313|EMBL:KRL28788.1, ECO:0000313|Proteomes:UP000051908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13238 {ECO:0000313|EMBL:KRL28788.1,
RC   ECO:0000313|Proteomes:UP000051908};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O.,
RA   Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E.,
RA   Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R.,
RA   Caufield P.W., Cui Y., Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through
RT   comparative genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRL28788.1}.
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DR   EMBL; AZES01000155; KRL28788.1; -; Genomic_DNA.
DR   RefSeq; WP_025085666.1; NZ_BAMH01000050.1.
DR   EnsemblBacteria; KRL28788; KRL28788; FD33_GL001489.
DR   PATRIC; fig|1122151.5.peg.1541; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000051908; 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:UP000051908};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:KRL28788.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138}.
FT   DOMAIN      107    312       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   418 AA;  46587 MW;  F6E0860A7E6AA8D1 CRC64;
     MKILVVGSGA REDAICQALQ KNSQNVVFCA PGNDGMKLSG IKTISIEEND FERMANFAQT
     NSIDYTVVGP EEPLVNGIVD FFKRQNLKIF GPNQQAAQVE GSKTFTKRLM ADAGIPTAQY
     QEFTKLEDAL NYLKIVSDFP IVIKADGLAA GKGVFIAPDL VAAAEVVTDL LAEHKFNTRR
     VVIEEYLEGE EFSLMVFVDH KRFYPMPLAQ DYKKILDGDL GPNTGGMGAV CPVANISKNI
     EQEAIENVLK PFVTELYDQG IKYTGILYAG LILTKKGIKV IEFNARFGDP ETEVVLPRLQ
     SDLSEIIEQI LCHKKIKKID WQIGGLNLGV FAVSKGYPIK PVFGSLGDRD TFKKCSLMIN
     YASVRREQQQ LYSHGGRLYL IQAQAETVED AQTKVYQELE KMDQTNIFYR RDIGKNSI
//
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