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Database: UniProt
Entry: A0A0A0BS30_9CELL
LinkDB: A0A0A0BS30_9CELL
Original site: A0A0A0BS30_9CELL 
ID   A0A0A0BS30_9CELL        Unreviewed;       430 AA.
AC   A0A0A0BS30;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   16-JAN-2019, entry version 22.
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=N869_00365 {ECO:0000313|EMBL:KGM09969.1};
OS   Cellulomonas bogoriensis 69B4 = DSM 16987.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM09969.1, ECO:0000313|Proteomes:UP000054314};
RN   [1] {ECO:0000313|EMBL:KGM09969.1, ECO:0000313|Proteomes:UP000054314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=69B4 {ECO:0000313|EMBL:KGM09969.1,
RC   ECO:0000313|Proteomes:UP000054314};
RA   Chen F., Li Y., Wang G.;
RT   "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL   Submitted (AUG-2013) 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:KGM09969.1}.
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DR   EMBL; AXCZ01000162; KGM09969.1; -; Genomic_DNA.
DR   RefSeq; WP_035062075.1; NZ_AXCZ01000162.1.
DR   EnsemblBacteria; KGM09969; KGM09969; N869_00365.
DR   OrthoDB; 932854at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000054314; 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:UP000054314};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:KGM09969.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054314}.
FT   DOMAIN      110    313       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   430 AA;  43575 MW;  25AD71BEF15C059D CRC64;
     MKILVIGSGA REHAVVRALA TGPEGPSGHE LHAAPGNPGI AALAELHDVD PVDPAAVAAL
     ATGLGAALVV VGPEAPLVAG VADAVREAGI PCFGPSAQAA ALEGSKAFAK EVMAAAEVPT
     AMAHVCTDLD QVAEALDAFG APYVVKDDGL AAGKGVVVTS DRDEALRHAA GCLDRRGGGG
     AVVIEEFLDG PEVSLFCLSD GRTVVPLAPA QDFKRALDGD EGPNTGGMGA YSPLPWAPAD
     LVQDVVARVA QPTVDEMYRR GTPFVGVLYC GLALTSRGVR VIEFNARFGD PETQVVLARL
     ASPLCEVLLA AATERLAEHP GLRWHADAAV TVVVAAHGYP GAVRAGDEIT GVDEAEQVPG
     AHVLHAGTAQ EGTGSLVSAG GRVLSVVGTG EDVDAARAVA YDAVARVGLR GSHHRTDIAA
     RMPVVEGPEA
//
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