ID   F7YWV9_9THEM            Unreviewed;       728 AA.
AC   F7YWV9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   03-APR-2013, entry version 14.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase 2;
DE            EC=6.3.5.3;
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase II;
GN   Name=purL; ORFNames=Theth_0458;
OS   Thermotoga thermarum DSM 5069.
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=688269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 5069;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermotoga thermarum DSM 5069.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D-
CC       ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-
CC       (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 1/2.
CC   -!- SUBUNIT: Heterodimer of two subunits, PurQ and PurL (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the FGAMS family.
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DR   EMBL; CP002351; AEH50551.1; -; Genomic_DNA.
DR   RefSeq; YP_004659647.1; NC_015707.1.
DR   EnsemblBacteria; AEH50551; AEH50551; Theth_0458.
DR   GeneID; 10885211; -.
DR   KEGG; tta:Theth_0458; -.
DR   KO; K01952; -.
DR   UniPathway; UPA00074; UER00128.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00420; PurL_2; 1; -.
DR   InterPro; IPR010918; AIR_synth_C_dom.
DR   InterPro; IPR000728; AIR_synth_N_dom.
DR   InterPro; IPR010074; PRibForGlyAmidine_synth_II.
DR   InterPro; IPR016188; PurM_N-like.
DR   Pfam; PF00586; AIRS; 2.
DR   Pfam; PF02769; AIRS_C; 2.
DR   SUPFAM; SSF56042; AIR_synth_C; 2.
DR   SUPFAM; SSF55326; PurM_N-like; 2.
DR   TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Purine biosynthesis.
FT   NP_BIND      97    108       ATP (By similarity).
SQ   SEQUENCE   728 AA;  79811 MW;  8E3E4444BF69A978 CRC64;
     MLKYRELGLN DEEYKKICQD LGREPNDVEL GMYSVTWSEH CSYKHSKPLL KLFPTSGKHV
     VQGPGENAGA VDIGDGLVVV FKMESHNHPS AVEPFQGAAT GVGGIVRDVL AMGARPIALL
     DSLRFGDIRK PNVKYLFNGV VGGISFYGNC IGVPTVAGEI YFNSCYDDNP LVNVMCVGIA
     RREELKFSRT GKTGARVLLV GALTGRDGIH GASFASQELD EESHSKRPSV QVGDPFMEKL
     LIEACLEACK VDGVLAVQDL GAAGLTSACS EVAAKSNKGI VIDLSKVPRR EANMSTYEVV
     LSESQERMLL IVEEKALQKV KEIFEKWDLV FSEIGYLTDD GFFTVYEGSE LVARVPVKSL
     TEGVPIVYIG PKERRLNVEE PNPPEPLNVQ DIFIKLLSSE NIASKRFVFE QYDHRVGINT
     VVLPGGDAAV LRIKGTNKGI AVSVDCNSLY CYVDPYEGGK IAVAEAARNV VVTGAKPLGI
     TDCLNFANPD DPEVYWELKR CIEGMAEAAK VLEIPIVSGN VSLYNESLKN RIYPTPTVGI
     VGLIEDISKR CSADFKSEND LVVLLGFHSD RFTASEYLRL IHNVEIAPSP TLDLEFEKRL
     QKVCLLAIKE GLLSSAHDVS EGGLAIALAE SSILGGFGVE CDLFTNVRKD VVLFSETQSR
     IVVSLPEKNF ERLKKLCETF KVPCTILGKI KGERFVIKIN GNKVIDVPLD EIIDLYMNSL
     ERKLNYEA
//