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Database: UniProt/SWISS-PROT
Entry: PURL_THEEB
LinkDB: PURL_THEEB
Original site: PURL_THEEB 
ID   PURL_THEEB              Reviewed;         761 AA.
AC   Q8DIA7;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   14-MAY-2014, entry version 78.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase 2;
DE            EC=6.3.5.3;
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase II;
DE            Short=FGAM synthase II;
GN   Name=purL; OrderedLocusNames=tlr1683;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
RA   Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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; BA000039; BAC09235.1; -; Genomic_DNA.
DR   RefSeq; NP_682473.1; NC_004113.1.
DR   ProteinModelPortal; Q8DIA7; -.
DR   STRING; 197221.tlr1683; -.
DR   EnsemblBacteria; BAC09235; BAC09235; BAC09235.
DR   GeneID; 1010851; -.
DR   KEGG; tel:tlr1683; -.
DR   PATRIC; 23928742; VBITheElo119873_1764.
DR   eggNOG; COG0046; -.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   OMA; QAVVFKI; -.
DR   OrthoDB; EOG6FNHHR; -.
DR   UniPathway; UPA00074; UER00128.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1330.10; -; 2.
DR   Gene3D; 3.90.650.10; -; 1.
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; SSF55326; SSF55326; 2.
DR   SUPFAM; SSF56042; SSF56042; 2.
DR   TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome.
FT   CHAIN         1    761       Phosphoribosylformylglycinamidine
FT                                synthase 2.
FT                                /FTId=PRO_0000100496.
FT   NP_BIND     105    116       ATP (Potential).
SQ   SEQUENCE   761 AA;  81412 MW;  CA1224C86FF8CE64 CRC64;
     MSQTPLVTEA EITAEGLKPQ EYTEIVRRLG RHPNRAELGM FGVMWSEHCC YKNSRLLLKQ
     FPTQGPRVLV GPGENAGVVD LGDGLRLAFK IESHNHPSAI EPFQGAATGV GGILRDIFTM
     GARPIALLNA LRFGDLKEAK TQQLVKGVVA GIAHYGNCVG VPTVGGEVYF DPCYAGNPLV
     NAMALGLMET PEIVKSAASG IGNPVLYVGS TTGRDGMGGA SFASAELTDE SMSDRPAVQV
     GDPFVEKCLI EACLEAFQTG AVVAAQDMGA AGLTCSTSEM AAKGGVGIEL DLDKVPVREQ
     GMVPYEFLLS ESQERMLFVA AQGREAELIE IFQRWGLQAV VVGRVIAEPL VRVLYRGEVA
     AEVPARALAE ETPLYERECP KEPPAYVQQA RQWSVDQLPL PARSPAEILL TLLATPSIAS
     KAWVYRQYDH EVQNNTLVFP GDGDAAVIRL RGTAKGIAAT VDCPSRYVYL DPYEGGKAAV
     AEAARNLSCV GAEPLAVTDN LNFGSPETPV GYWQLANACR GLAEACRALQ TPVTGGNVSL
     YNETIDSNGQ PQPIYPTPVV GMVGLIADLQ RVVGQGWRAT GDAIYLLGLP LTTPLSDPRL
     SLGGSEYLAQ IHGLVAGCPP QIDLDLEQRV QAVCRYGIQQ GWIASAHDLS EGGLAVALAE
     SCLSGQRGAT IQLPEGTYPR WDALLFAEGG ARILVSVPPR EQVAWEAYAQ AQLPNAWTRL
     GVVNGEDTEL CIDSCNNSPL IRVTIKELDL AWRSPLPKYL D
//
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