ID   PUR2_METST              Reviewed;         438 AA.
AC   Q2NI86;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=Msp_0030;
OS   Methanosphaera stadtmanae (strain DSM 3091).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H.,
RA   Hedderich R., Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this
RT   human intestinal archaeon is restricted to methanol and H2 for methane
RT   formation and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC56449.1; -; Genomic_DNA.
DR   RefSeq; YP_447092.1; -.
DR   GeneID; 3855038; -.
DR   GenomeReviews; CP000102_GR; Msp_0030.
DR   KEGG; mst:Msp_0030; -.
DR   NMPDR; fig|339860.6.peg.29; -.
DR   HOGENOM; Q2NI86; -.
DR   OMA; Q2NI86; IEYNCRF.
DR   BioCyc; MSTA339860:MSP_0030-MON; -.
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_1000018829.
FT   DOMAIN      107    319       ATP-grasp.
FT   NP_BIND     134    197       ATP (By similarity).
FT   METAL       277    277       Magnesium or manganese 1 (By similarity).
FT   METAL       289    289       Magnesium or manganese 1 (By similarity).
FT   METAL       289    289       Magnesium or manganese 2 (By similarity).
FT   METAL       291    291       Magnesium or manganese 2 (By similarity).
SQ   SEQUENCE   438 AA;  48794 MW;  C59F9094D2DA0186 CRC64;
     MKILMVGSGA REHAIAKALN KTADVYTYMG RKNPGLARIS KNYTVNDESN FNEIIKFAQE
     NNVELAFIGP EAPLEMGIVD ELEKEGIHSV GPTKSAAQIE TNKAFMRKLF EDYDIPGSIK
     YGTFYDLDEA YEFIDNFDEP VVVKPIGLTG GKGVKIVGDQ LADNDEAKEY VKEIFHQKMG
     GFEGVVIEEL LLGEEYTIQA FVDGTHLIPM PAAQDHPHAF VGNKGPITGG MGSYSDKNHL
     LPFLTQEDYD KSVEIMEKTI KAIAKEQEPY KGILYGQFML CKDGPKVIEY NARFGDPESM
     NVLSVIDDDL AKISKQIVDG TLDSVNFLNK SSVCKYVVPD KYPNTHVADT VVDVDEDKIN
     ELGAQVFYAA VYQDMDDSIK LTSSRALGVL AVKDSIKEAE KICEEAIKYV KGEVYHRNDV
     ATEELLNEKI KHMEEVRL
//