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Database: UniProt
Entry: M4X1B5_9PSED
LinkDB: M4X1B5_9PSED
Original site: M4X1B5_9PSED 
ID   M4X1B5_9PSED            Unreviewed;       429 AA.
AC   M4X1B5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   10-APR-2019, entry version 41.
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=D0N87_02735 {ECO:0000313|EMBL:RFQ40951.1}, H681_21730
GN   {ECO:0000313|EMBL:AGI26213.1};
OS   Pseudomonas sp. ATCC 13867.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1294143 {ECO:0000313|EMBL:AGI26213.1, ECO:0000313|Proteomes:UP000012082};
RN   [1] {ECO:0000313|EMBL:AGI26213.1, ECO:0000313|Proteomes:UP000012082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13867 {ECO:0000313|EMBL:AGI26213.1,
RC   ECO:0000313|Proteomes:UP000012082};
RX   PubMed=23723394;
RA   Ainala S.K., Somasundar A., Park S.;
RT   "Complete genome sequence of Pseudomonas denitrificans ATCC 13867.";
RL   Genome Announc. 1:E00257-13(2013).
RN   [2] {ECO:0000313|EMBL:RFQ40951.1, ECO:0000313|Proteomes:UP000260857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13867 {ECO:0000313|EMBL:RFQ40951.1,
RC   ECO:0000313|Proteomes:UP000260857};
RA   Meier M.J., Dodge A., Beaudette L.A.;
RT   "Draft genome of the industrially relevant bacterium Pseudomonas
RT   denitrificans ATCC 13867.";
RL   Submitted (AUG-2018) 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; CP004143; AGI26213.1; -; Genomic_DNA.
DR   EMBL; QVNC01000012; RFQ40951.1; -; Genomic_DNA.
DR   RefSeq; WP_015479063.1; NC_020829.1.
DR   STRING; 1294143.H681_21730; -.
DR   EnsemblBacteria; AGI26213; AGI26213; H681_21730.
DR   GeneID; 32561305; -.
DR   KEGG; pdr:H681_21730; -.
DR   PATRIC; fig|1294143.3.peg.4407; -.
DR   KO; K01945; -.
DR   OrthoDB; 932854at2; -.
DR   BioCyc; PDEN1294143:G1HG9-4437-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000012082; Chromosome.
DR   Proteomes; UP000260857; 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:UP000012082,
KW   ECO:0000313|Proteomes:UP000260857};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:AGI26213.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138}.
FT   DOMAIN      108    315       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   429 AA;  45424 MW;  FCA6C6E9E1580A75 CRC64;
     MNVLIIGSGG REHALAWKVA QDSRVQKVFV APGNAGTATE AKCENVAIDV LALEELADFA
     AKNVQLTIVG PEAPLVKGVV DLFRARGLDI FGPTAGAAQL EGSKAFTKDF LARHQIPTAD
     YQNFTEVEPA LAYLKEKGAP IVIKADGLAA GKGVIVAMTL QEAEDAVRDM LAGNAFGDAG
     SRVVIEEFLD GEEASFIVMV DGQNVLPMAT SQDHKRVGDA DTGPNTGGMG AYSPAPVVTP
     DVHKRVMDEV IYPTVRGMAE EGNVYTGFLY AGLMIDKSGA PKVIEFNCRF GDPETQPIMV
     RLESSLVLLV EAALAKALDK VEATWDPRPT VGVVLAAGGY PGDYAKGDVI EGLDEAAKLD
     GKVFHAGTAL KDGQIVTSGG RVLCATAIGP NVSSAQEQAY RLAEKIRWNG CFYRKDIGYR
     AIARERGEG
//
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