ID A1AIH6_ECOK1 Unreviewed; 429 AA.
AC A1AIH6;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 01-MAY-2013, entry version 50.
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=Ecok1_39720; ORFNames=APECO1_2470;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/JB.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain
RT O1:K1:H7 shares strong similarities with human extraintestinal
RT pathogenic E. coli genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
CC -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP
CC + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
CC -!- COFACTOR: Binds (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 (By similarity).
CC -!- SIMILARITY: Belongs to the GARS family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR EMBL; CP000468; ABJ03466.1; -; Genomic_DNA.
DR RefSeq; YP_859590.1; NC_008563.1.
DR ProteinModelPortal; A1AIH6; -.
DR SMR; A1AIH6; 1-426.
DR STRING; 405955.APECO1_2470; -.
DR EnsemblBacteria; ABJ03466; ABJ03466; APECO1_2470.
DR GeneID; 4492855; -.
DR KEGG; ecv:APECO1_2470; -.
DR PATRIC; 18220547; VBIEscCol127180_4475.
DR eggNOG; COG0151; -.
DR HOGENOM; HOG000033463; -.
DR KO; K01945; -.
DR OMA; MGAYTPL; -.
DR ProtClustDB; PRK00885; -.
DR UniPathway; UPA00074; UER00125.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA: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; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 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.
FT DOMAIN 109 316 ATP-grasp (By similarity).
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).
SQ SEQUENCE 429 AA; 45946 MW; FEA96662C44CD6D9 CRC64;
MKVLVIGNGG REHALAWKAA QSPLVETVFV APGNAGTALE PALQNVAIGV TDIPALLDFA
QNEKVDLTIV GPEAPLVKGV VDTFRAAGLK IFGPTAGAAQ LEGSKAFTKD FLARHNIPTA
EYQNFTEVEP ALAYLREKGA PIVIKADGLA AGKGVIVAMT LEEAEAAVRD MLAGNAFGDA
GHRIVIEEFL DGEEASFIVM VDGEHVLPMA TSQDHKRVGD KDTGPNTGGM GAYSPAPVVT
DEVHQRTMER IIWPTVKGMA AEGNTYTGFL YAGLMIDKQG NPKVIEFNCR FGDPETQPIM
LRMKSDLVEL CLAACEGKLD EKTSEWDERA SLGVVMAAGG YPGDYRTGDV IHGLPLEEVA
DGKVFHAGTK LADDEQVVTS GGRVLCVTAL GHTVAEAQKR AYALMTDIHW DDCFCRKDIG
WRAIEREQN
//
