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Database: UniProt
Entry: A0A1C2G3P1_9GAMM
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ID   A0A1C2G3P1_9GAMM        Unreviewed;       424 AA.
AC   A0A1C2G3P1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   31-JUL-2019, entry version 17.
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=A9R16_08045 {ECO:0000313|EMBL:OCX46119.1}, C4900_00420
GN   {ECO:0000313|EMBL:RCN58301.1};
OS   Acidiferrobacter thiooxydans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Acidiferrobacterales;
OC   Acidiferrobacteraceae; Acidiferrobacter.
OX   NCBI_TaxID=163359 {ECO:0000313|EMBL:OCX46119.1};
RN   [1] {ECO:0000313|EMBL:OCX46119.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZJ {ECO:0000313|EMBL:OCX46119.1};
RA   Ma L.;
RT   "Draft Genome Sequence of Acidiferrobacter thiooxydans ZJ, a
RT   Distinctive Species of Ectothiorhodospiraceae.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RCN58301.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M-1 {ECO:0000313|EMBL:RCN58301.1};
RA   Issotta F., Thyssen C., Mena C., Moya A., Bellenberg S., Sproer C.,
RA   Covarrubias P.C., Sand W., Quatrini R., Vera M.;
RT   "Insights into the biology of acidophilic members of the
RT   Acidiferrobacteraceae family derived from comparative genomic
RT   analyses.";
RL   Submitted (FEB-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}.
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:OCX46119.1}.
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DR   EMBL; MDCF01000041; OCX46119.1; -; Genomic_DNA.
DR   EMBL; PSYR01000001; RCN58301.1; -; Genomic_DNA.
DR   RefSeq; WP_065969019.1; NZ_PSYR01000001.1.
DR   EnsemblBacteria; OCX46119; OCX46119; A9R16_08045.
DR   BioCyc; GCF_001705075:A9R16_RS02305-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
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   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:OCX46119.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138}.
FT   DOMAIN      109    314       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION      212    232       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   424 AA;  44692 MW;  86206108A237E0E4 CRC64;
     MKILIVGSGG REHALAWKAA QSPLASEVLV APGNAGTARE PKIRNCPVAA TDIAALIDLA
     RRERVDLTIV GPEAPLVAGI VDRFTEEGLA CLGPTAAAAR LEGSKSFAKA FLARHGIPTA
     RHETFSDQAA AARYLKDHPG AHVVKADGLA SGKGVVVAED EATALAAATA MLNGEFGEAG
     RRIVIEERLI GVEASFIVLA CGLDYVAFPT SEDHKRRDDG DRGPNTGGMG AFSPASAVDA
     ALEIVIRREI IEPTLRGLKA DGHHYCGFLY AGLMLTADGP RVLEYNCRFG DPETQPIMMR
     LRSDLVALTQ AAVHGRLGGE TLEIDPRPAL CVVLAAPGYP ADPRTGDMIA GLDAADPQTK
     VFHAGTRELD GQVLSSGGRV LGVTSLGATL EEAREHVYRR LGTIALDGAL YRHDIGRRPY
     GVKP
//
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