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Database: UniProt
Entry: A0A1Q2CCE3_9ACTN
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ID   A0A1Q2CCE3_9ACTN        Unreviewed;       408 AA.
AC   A0A1Q2CCE3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   13-FEB-2019, entry version 10.
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=RPIT_01905 {ECO:0000313|EMBL:AQP43715.1}, SAMN05428934_108129
GN   {ECO:0000313|EMBL:SDZ03424.1};
OS   Tessaracoccus flavus.
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Tessaracoccus.
OX   NCBI_TaxID=1610493 {ECO:0000313|EMBL:AQP43715.1, ECO:0000313|Proteomes:UP000188324};
RN   [1] {ECO:0000313|EMBL:AQP43715.1, ECO:0000313|Proteomes:UP000188324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RP1T {ECO:0000313|EMBL:AQP43715.1,
RC   ECO:0000313|Proteomes:UP000188324};
RX   PubMed=26869509; DOI=10.1099/ijsem.0.000958;
RA   Kumari R., Singh P., Schumann P., Lal R.;
RT   "Tessaracoccus flavus sp. nov., isolated from the drainage system of a
RT   lindane-producing factory.";
RL   Int. J. Syst. Evol. Microbiol. 66:1862-1868(2016).
RN   [2] {ECO:0000313|EMBL:SDZ03424.1, ECO:0000313|Proteomes:UP000199635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RP1 {ECO:0000313|EMBL:SDZ03424.1,
RC   ECO:0000313|Proteomes:UP000199635};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AQP43715.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RP1T {ECO:0000313|EMBL:AQP43715.1};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; CP019605; AQP43715.1; -; Genomic_DNA.
DR   EMBL; FNPU01000008; SDZ03424.1; -; Genomic_DNA.
DR   KEGG; tfl:RPIT_01905; -.
DR   KO; K01945; -.
DR   BioCyc; GCF_001997295:RPIT_RS01875-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000188324; Chromosome.
DR   Proteomes; UP000199635; 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:UP000188324,
KW   ECO:0000313|Proteomes:UP000199635};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:AQP43715.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188324}.
FT   DOMAIN      107    303       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   408 AA;  42419 MW;  09B313E9C90D8613 CRC64;
     MKILLLGSGG REHAIGRALA HDPAVTELHV APGNPGLSSI ATMHSADPAS PTAVLDLARS
     LQVDLIVIGP EAPLVAGVAD ALRDAGFDVF GPGREAAVLE GSKAFAKEVM RSAGVPTADA
     RVCETPDEVS AALDEFGPPY VVKNDGLAAG KGVVVTTDRQ EALDHAASCG RVVIEDFLDG
     PEVSLFAICD GERALPLLPA QDYKRVGDDD EGPNTGGMGA YCPLSWADAG LTDQIMSEVV
     NPTLAEMRRR GTPFIGLLYA GLALTSRGLR VVEFNVRFGD PETQAVLSLL KTPLAGVLRA
     AARGELDSVP ELDWHDGAAV VVVSAAEGYP GTPATGRPIT LPDDETDAYV LHAGTRIEGG
     RLVSSGGRVL GIVGRGADLD EARRLAYALL ERIDFAGGFS RTDIGVPH
//
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