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Database: UniProt
Entry: U2YV59_9CAUL
LinkDB: U2YV59_9CAUL
Original site: U2YV59_9CAUL 
ID   U2YV59_9CAUL            Unreviewed;       425 AA.
AC   U2YV59;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   03-JUL-2019, entry version 31.
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=MBEBAB_1596 {ECO:0000313|EMBL:GAD59346.1};
OS   Brevundimonas abyssalis TAR-001.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1391729 {ECO:0000313|EMBL:GAD59346.1, ECO:0000313|Proteomes:UP000016569};
RN   [1] {ECO:0000313|EMBL:GAD59346.1, ECO:0000313|Proteomes:UP000016569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAR-001 {ECO:0000313|EMBL:GAD59346.1,
RC   ECO:0000313|Proteomes:UP000016569};
RA   Tsubouchi T., Nishi S., Usui K., Shimane Y., Takaki Y., Maruyama T.,
RA   Hatada Y.;
RT   "Draft Genome Sequence of the Dimorphic Prosthecate Bacterium
RT   Brevundimonas abyssalis TAR-001T.";
RL   Genome Announc. 1:e00826-13(2013).
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:GAD59346.1}.
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DR   EMBL; BATC01000024; GAD59346.1; -; Genomic_DNA.
DR   RefSeq; WP_021697441.1; NZ_BATC01000024.1.
DR   EnsemblBacteria; GAD59346; GAD59346; MBEBAB_1596.
DR   OrthoDB; 932854at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000016569; 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:UP000016569};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:GAD59346.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016569}.
FT   DOMAIN      107    312       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   425 AA;  44651 MW;  EAAD7BE5B6C99638 CRC64;
     MKVLLVGSGG REHALAWKIR QSPLVTSLVI APGNPGMERL GELAPVKADD AEGLAALARE
     IRADLVVVGP EMALAAGLAD RLAAAGIPCF GPTARAAQLE TSKAFAKDFL ERHNIPTAGY
     GVYETLAEAR QALDVFRPPY VIKADGLAAG KGVAISPDRP DAEAEIERML GGRFGAAGAR
     VVIEEFMDGE EGSLFALCDG TRAVLLGGAQ DHKRAFDGDL GPNTGGMGAY SPAPVFTPEL
     VQQADERVIQ PTMAGMAAEG APYRGVLYAG LMATADGPKV VEFNARFGDP ECQVLMMRLA
     GDIVPHLLAC ARGDVSKLPP LEFRPETVIC VVMAAKGYPD SPLTGSVIRG ADQDFGPDVE
     VFHAGTARNK DGALVASGGR VLNVCARGAD IAQARERAYA AISRIDWPGG FHRSDIGWRA
     LDRDD
//
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