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Database: UniProt/SWISS-PROT
Entry: PURL_THET2
LinkDB: PURL_THET2
Original site: PURL_THET2 
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-OCT-2014, entry version 70.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE            Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00420};
DE            EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00420};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
DE            Short=FGAR amidotransferase II {ECO:0000255|HAMAP-Rule:MF_00420};
DE            Short=FGAR-AT II {ECO:0000255|HAMAP-Rule:MF_00420};
DE   AltName: Full=Glutamine amidotransferase PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
GN   Name=purL {ECO:0000255|HAMAP-Rule:MF_00420};
GN   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   -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC       complex involved in the purines biosynthetic pathway. Catalyzes
CC       the ATP-dependent conversion of formylglycinamide ribonucleotide
CC       (FGAR) and glutamine to yield formylglycinamidine ribonucleotide
CC       (FGAM) and glutamate. The FGAM synthase complex is composed of
CC       three subunits. PurQ produces an ammonia molecule by converting
CC       glutamine to glutamate. PurL transfers the ammonia molecule to
CC       FGAR to form FGAM in an ATP-dependent manner. PurS interacts with
CC       PurQ and PurL and is thought to assist in the transfer of the
CC       ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP-
CC       Rule:MF_00420}.
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       {ECO:0000255|HAMAP-Rule:MF_00420}.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00420}.
CC   -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1
CC       PurL, 1 PurQ and 2 PurS subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00420}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}.
CC   -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00420}.
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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; MIAVAEC; -.
DR   OrthoDB; EOG6FNHHR; -.
DR   BioCyc; TTHE262724:GCAT-1168-MONOMER; -.
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:0000287; F:magnesium ion 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   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; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN         1    725       Phosphoribosylformylglycinamidine
FT                                synthase subunit PurL.
FT                                /FTId=PRO_0000100502.
FT   REGION       86     89       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   REGION      303    305       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   ACT_SITE     41     41       {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   ACT_SITE     87     87       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL        85     85       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       109    109       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       259    259       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       523    523       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING      44     44       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING      83     83       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     108    108       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     231    231       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     485    485       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     522    522       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     525    525       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
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
//
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