ID   PUR2_PYRHO              Reviewed;         438 AA.
AC   O58061;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 60.
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=PH0323;
OS   Pyrococcus horikoshii.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=53953;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT3;
RX   MEDLINE=98344137; PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y.,
RA   Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y.,
RA   Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K.,
RA   Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP
CC       + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
CC   -!- COFACTOR: Binds 2 magnesium or manganese ions 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   -!- SIMILARITY: Belongs to the GARS family.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR   EMBL; BA000001; BAA29397.1; -; Genomic_DNA.
DR   PIR; H71138; H71138.
DR   RefSeq; NP_142306.1; -.
DR   HSSP; P15640; 1GSO.
DR   GeneID; 1444205; -.
DR   GenomeReviews; BA000001_GR; PH0323.
DR   KEGG; pho:PH0323; -.
DR   NMPDR; fig|70601.1.peg.305; -.
DR   HOGENOM; O58061; -.
DR   OMA; O58061; IEYNCRF.
DR   BRENDA; 6.3.4.13; 74679.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:HAMAP.
DR   GO; GO:0009113; P:purine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00138; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR000115; Gars.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 1.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 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   CHAIN         1    438       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151516.
FT   DOMAIN      108    316       ATP-grasp.
FT   NP_BIND     135    194       ATP (By similarity).
FT   METAL       274    274       Magnesium or manganese 1 (By similarity).
FT   METAL       286    286       Magnesium or manganese 1 (By similarity).
FT   METAL       286    286       Magnesium or manganese 2 (By similarity).
FT   METAL       288    288       Magnesium or manganese 2 (By similarity).
SQ   SEQUENCE   438 AA;  48458 MW;  396EED8AF69A7805 CRC64;
     MKVLLVGGGG REHAIGEALV KGGAELYVVS NHRNPGLMRL AKDYGLAKET NVEDVIKFAR
     KWGIELAFIG PEAPLEAGIV NALEEEGIPA VGPTREAARL ETNKAWAREF MERNNIPGRK
     MFRIFDDVQE MRKWIDEYGK PVVVKPLGLT GGKGVKVVGY QLKDNEEAKE YAEHIIRKDG
     KVLIEERTDG VEFTLQVFTD GKKVIPMPLV QDYPHAYEGD VGPITGGMGS YSCSNHLLPF
     ITEGDFERAL KTLEETIEAM RKEGYPYKGI LYGQFMLSGE GPVLIEYNAR FGDPEAINVL
     AVLDDNLLEI AKGIVEGSLR KAKFLNKATV VKYIAPQGYP QDPIKGIRIE VDEEGIKNEG
     AKIIYAAVDE NLTLLGSRAL AIVGVADSLE EAERIAENGV SYVKGPIFYR KDVGTRESVE
     KRIEIMKKLG KEFEPNLC
//