ID PURL_THET2 Reviewed; 725 AA.
AC Q72IH7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 01-MAY-2013, entry version 62.
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=TT_C1155;
OS Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB27 / ATCC BAA-163 / DSM 7039;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T.,
RA Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R.,
RA Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R.,
RA Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus
RT thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AE017221; AAS81497.1; -; Genomic_DNA.
DR RefSeq; YP_005124.1; NC_005835.1.
DR ProteinModelPortal; Q72IH7; -.
DR STRING; 262724.TTC1155; -.
DR EnsemblBacteria; AAS81497; AAS81497; TT_C1155.
DR GeneID; 2774749; -.
DR KEGG; tth:TTC1155; -.
DR PATRIC; 23952719; VBITheThe54392_1149.
DR eggNOG; COG0046; -.
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 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.
FT CHAIN 1 725 Phosphoribosylformylglycinamidine
FT synthase 2.
FT /FTId=PRO_0000100502.
FT NP_BIND 98 109 ATP (Potential).
SQ SEQUENCE 725 AA; 78643 MW; C5CC5FAE833F0199 CRC64;
MEALAKEIGI PEGEYREIVQ RLGREPNRVE LLLFKVMWSE HCAYKNSRPL LKALPKEGEA
VLQGPGENAG VVRVGEGWAV AFKIESHNHP SAVEPFQGAA TGVGGILRDI MSMGARPIAL
LDSLRFGPPE EARSRYLLKG VVSGIAFYGN AIGVPTVGGD LYFHEGYREN PLVNAMCLGL
LREEHLKRSR ASLGRPIYYA GAKTGRDGIG GAAFASRELK EEKAEDRPAV QVGDPFLGKL
LMEATLEAIE LDLVEGVQDM GAAGLTSSLS ELAHKSGLGV ELHLDLVPTR EEGMTPEELL
LSESQERMVL VPKEGKEKAL EEVFGRWGLD CVPVARTIPE RVFRVLFRGE VVAEVPTEAL
AEAPTYVRVG REDPEVRRLR ETPIPPLEAD PQEVLRRLLA SPNLASREAV YERYDHQVGT
RTALLPGKGD AAVLWIKGTR LGVAAKVDQN PRYSRLHPRL GAMHALAEAC RNVSVVGAKP
LAYTDGLNLG SPETPEGYHE LAETIAGLKE ASEALGVPVV SGNVSLYNES GGKRIPPTAM
VGVVGVLEVD KRAEMGFRRP GEVLLLIGEE RGELGASEVL YLLTGKEFGH PPRLDLGREK
AVQEAIRDLI QRGLTRTAHD VAEGGLLLAL AEMTFPYGVG ATVEVREEGL EALFGEAPSR
VLFTVEKTRL QEATLLLEER GLPYRVLGET GGKSLTVLTP GGVLEWSLEE LLSAWKAPLR
EVLDG
//
