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Database: UniProt/SWISS-PROT
Entry: PUR2_STRCO
LinkDB: PUR2_STRCO
Original site: PUR2_STRCO 
ID   PUR2_STRCO              Reviewed;         416 AA.
AC   Q9RKL4;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   29-OCT-2014, entry version 86.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000255|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000255|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000255|HAMAP-Rule:MF_00138};
GN   OrderedLocusNames=SCO4068; ORFNames=SCD25.04;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces;
OC   Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP
CC       + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
CC       {ECO:0000255|HAMAP-Rule:MF_00138}.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit.
CC       {ECO:0000250}.
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:0000255|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00138}.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00138}.
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DR   EMBL; AL939118; CAB56348.1; -; Genomic_DNA.
DR   RefSeq; NP_628249.1; NC_003888.3.
DR   ProteinModelPortal; Q9RKL4; -.
DR   STRING; 100226.SCO4068; -.
DR   PRIDE; Q9RKL4; -.
DR   EnsemblBacteria; CAB56348; CAB56348; CAB56348.
DR   GeneID; 1099505; -.
DR   KEGG; sco:SCO4068; -.
DR   PATRIC; 23737902; VBIStrCoe124346_4127.
DR   eggNOG; COG0151; -.
DR   HOGENOM; HOG000033463; -.
DR   InParanoid; Q9RKL4; -.
DR   KO; K01945; -.
DR   OMA; YKGFLYA; -.
DR   OrthoDB; EOG69SKD1; -.
DR   PhylomeDB; Q9RKL4; -.
DR   UniPathway; UPA00074; UER00125.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 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; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
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   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; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    416       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151486.
FT   DOMAIN      107    303       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     133    184       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       273    273       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       275    275       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   416 AA;  42623 MW;  21715503DEEF70B3 CRC64;
     MKVLVIGGGA REHALCRSLS LDPDVTALHC APGNAGIAEV AELHQVDALD GAAVTALAGR
     LGAELVVVGP EAPLVAGVAD AVREAGIPVF GPSGEAARLE GSKAFAKDVM ACAGVPTARS
     YVCTNPAEVD AALAAFGAPY VVKDDGLAAG KGVVVTDDVE AARAHANACD RVVVEEFLDG
     PEVSLFAVTD GENVRPLQPA QDFKRALDGD EGPNTGGMGA YSPLPWADPK LVDEVVQSVL
     QPTVDEMRRR GTPFSGLLYA GLAITSRGVR VIEFNARFGD PETQVVLARL KTPLAGLLMA
     AATGNLADLE PLRWSDEAAV TVVVASHNYP GTPRTGDPIT GLDEVAAQDA PHAYVLHAGT
     RAEGDAVVSA GGRVLSVTAT GADLTEARDR AYRAVARIGL DGSQHRTDIA AKAAGA
//
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