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Database: UniProt
Entry: P15640
LinkDB: P15640
Original site: P15640 
ID   PUR2_ECOLI              Reviewed;         429 AA.
AC   P15640; Q2M8U2;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   16-APR-2014, entry version 130.
DE   RecName: Full=Phosphoribosylamine--glycine ligase;
DE            EC=6.3.4.13;
DE   AltName: Full=GARS;
DE   AltName: Full=Glycinamide ribonucleotide synthetase;
DE   AltName: Full=Phosphoribosylglycinamide synthetase;
GN   Name=purD; OrderedLocusNames=b4005, JW3969;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2687276;
RA   Aiba A., Mizobuchi K.;
RT   "Nucleotide sequence analysis of genes purH and purD involved in the
RT   de novo purine nucleotide biosynthesis of Escherichia coli.";
RL   J. Biol. Chem. 264:21239-21246(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2182115; DOI=10.1021/bi00453a030;
RA   Shen Y., Rudolph J., Stern M., Flannigan K.A., Smith J.M.;
RT   "Glycinamide ribonucleotide synthetase from Escherichia coli: cloning,
RT   overproduction, sequencing, isolation, and characterization.";
RL   Biochemistry 29:218-227(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
RA   Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the
RT   region from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=9843369; DOI=10.1021/bi981405n;
RA   Wang W., Kappock T.J., Stubbe J., Ealick S.E.;
RT   "X-ray crystal structure of glycinamide ribonucleotide synthetase from
RT   Escherichia coli.";
RL   Biochemistry 37:15647-15662(1998).
CC   -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP
CC       + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
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.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the GARS family.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR   EMBL; J05126; AAA24455.1; -; Genomic_DNA.
DR   EMBL; X51950; CAA36213.1; -; Genomic_DNA.
DR   EMBL; U00006; AAC43103.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76979.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77314.1; -; Genomic_DNA.
DR   PIR; A33771; AJECQG.
DR   RefSeq; NP_418433.1; NC_000913.3.
DR   RefSeq; YP_491455.1; NC_007779.1.
DR   PDB; 1GSO; X-ray; 1.60 A; A=1-429.
DR   PDBsum; 1GSO; -.
DR   ProteinModelPortal; P15640; -.
DR   SMR; P15640; 1-426.
DR   IntAct; P15640; 4.
DR   STRING; 511145.b4005; -.
DR   SWISS-2DPAGE; P15640; -.
DR   PaxDb; P15640; -.
DR   PRIDE; P15640; -.
DR   EnsemblBacteria; AAC76979; AAC76979; b4005.
DR   EnsemblBacteria; BAE77314; BAE77314; BAE77314.
DR   GeneID; 12933468; -.
DR   GeneID; 948504; -.
DR   KEGG; ecj:Y75_p3191; -.
DR   KEGG; eco:b4005; -.
DR   PATRIC; 32123535; VBIEscCol129921_4120.
DR   EchoBASE; EB0785; -.
DR   EcoGene; EG10792; purD.
DR   eggNOG; COG0151; -.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   OMA; DPEAMNV; -.
DR   OrthoDB; EOG69SKD1; -.
DR   PhylomeDB; P15640; -.
DR   ProtClustDB; PRK00885; -.
DR   BioCyc; EcoCyc:GLYCRIBONUCSYN-MONOMER; -.
DR   BioCyc; ECOL316407:JW3969-MONOMER; -.
DR   BioCyc; MetaCyc:GLYCRIBONUCSYN-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   EvolutionaryTrace; P15640; -.
DR   PRO; PR:P15640; -.
DR   Genevestigator; P15640; -.
DR   GO; GO:0005524; F:ATP binding; IDA:EcoliWiki.
DR   GO; GO:0042623; F:ATPase activity, coupled; IDA:EcoliWiki.
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; IDA:EcoCyc.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006200; P:ATP catabolic process; IDA:GOC.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; NAS:EcoliWiki.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Ligase; Magnesium;
KW   Manganese; Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    429       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151448.
FT   DOMAIN      109    316       ATP-grasp.
FT   NP_BIND     135    196       ATP (By similarity).
FT   METAL       286    286       Magnesium or manganese (By similarity).
FT   METAL       288    288       Magnesium or manganese (By similarity).
FT   CONFLICT     15     16       LA -> WR (in Ref. 1; AAA24455).
FT   CONFLICT     97     97       G -> V (in Ref. 1; AAA24455).
FT   STRAND        1      7
FT   HELIX        10     19
FT   STRAND       25     32
FT   HELIX        35     39
FT   STRAND       43     45
FT   HELIX        53     62
FT   STRAND       66     70
FT   HELIX        73     77
FT   HELIX        80     86
FT   STRAND       91     93
FT   TURN         96     99
FT   HELIX       100    103
FT   HELIX       105    114
FT   STRAND      122    129
FT   HELIX       130    138
FT   STRAND      140    145
FT   STRAND      155    160
FT   HELIX       161    168
FT   TURN        169    172
FT   STRAND      184    188
FT   STRAND      192    204
FT   STRAND      206    219
FT   TURN        220    222
FT   STRAND      223    235
FT   HELIX       241    250
FT   HELIX       252    261
FT   STRAND      267    277
FT   STRAND      282    290
FT   TURN        293    295
FT   HELIX       296    302
FT   HELIX       307    315
FT   HELIX       319    321
FT   STRAND      328    338
FT   TURN        339    342
FT   STRAND      362    371
FT   STRAND      377    379
FT   STRAND      381    393
FT   HELIX       394    404
FT   TURN        405    407
FT   HELIX       421    425
SQ   SEQUENCE   429 AA;  45940 MW;  5E9EFAD478BC1FF4 CRC64;
     MKVLVIGNGG REHALAWKAA QSPLVETVFV APGNAGTALE PALQNVAIGV TDIPALLDFA
     QNEKIDLTIV GPEAPLVKGV VDTFRAAGLK IFGPTAGAAQ LEGSKAFTKD FLARHKIPTA
     EYQNFTEVEP ALAYLREKGA PIVIKADGLA AGKGVIVAMT LEEAEAAVHD MLAGNAFGDA
     GHRIVIEEFL DGEEASFIVM VDGEHVLPMA TSQDHKRVGD KDTGPNTGGM GAYSPAPVVT
     DDVHQRTMER IIWPTVKGMA AEGNTYTGFL YAGLMIDKQG NPKVIEFNCR FGDPETQPIM
     LRMKSDLVEL CLAACESKLD EKTSEWDERA SLGVVMAAGG YPGDYRTGDV IHGLPLEEVA
     GGKVFHAGTK LADDEQVVTN GGRVLCVTAL GHTVAEAQKR AYALMTDIHW DDCFCRKDIG
     WRAIEREQN
//
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