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 29-MAY-2013, entry version 73.
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; WSEHCCY; -.
DR ProtClustDB; PRK01213; -.
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 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; 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; 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
//