PURL_THET8
ID PURL_THET8 Reviewed; 725 AA.
AC Q5SMH8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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}; OrderedLocusNames=TTHA1519;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH ADP; MAGNESIUM AND
RP PHOSPHATE.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=22232163; DOI=10.1107/s1744309111048184;
RA Suzuki S., Yanai H., Kanagawa M., Tamura S., Watanabe Y., Fuse K., Baba S.,
RA Sampei G., Kawai G.;
RT "Structure of N-formylglycinamide ribonucleotide amidotransferase II (PurL)
RT from Thermus thermophilus HB8.";
RL Acta Crystallogr. F 68:14-19(2012).
CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC complex involved in the purines biosynthetic pathway. Catalyzes the
CC ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and
CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and
CC glutamate. The FGAM synthase complex is composed of three subunits.
CC PurQ produces an ammonia molecule by converting glutamine to glutamate.
CC PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-
CC dependent manner. PurS interacts with PurQ and PurL and is thought to
CC assist in the transfer of the ammonia molecule from PurQ to PurL.
CC {ECO:0000255|HAMAP-Rule:MF_00420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00420};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC 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 PurL,
CC 1 PurQ and 2 PurS subunits. {ECO:0000255|HAMAP-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; AP008226; BAD71342.1; -; Genomic_DNA.
DR RefSeq; WP_011173566.1; NC_006461.1.
DR RefSeq; YP_144785.1; NC_006461.1.
DR PDB; 3VIU; X-ray; 2.35 A; A=1-725.
DR PDBsum; 3VIU; -.
DR AlphaFoldDB; Q5SMH8; -.
DR SMR; Q5SMH8; -.
DR STRING; 300852.55772901; -.
DR EnsemblBacteria; BAD71342; BAD71342; BAD71342.
DR GeneID; 3168862; -.
DR KEGG; ttj:TTHA1519; -.
DR PATRIC; fig|300852.9.peg.1494; -.
DR eggNOG; COG0046; Bacteria.
DR HOGENOM; CLU_003100_0_1_0; -.
DR OMA; FIEPYQG; -.
DR PhylomeDB; Q5SMH8; -.
DR UniPathway; UPA00074; UER00128.
DR EvolutionaryTrace; Q5SMH8; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.90.650.10; -; 2.
DR HAMAP; MF_00420; PurL_2; 1.
DR InterPro; IPR010074; PRibForGlyAmidine_synth_PurL.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR PANTHER; PTHR43555; PTHR43555; 1.
DR Pfam; PF00586; AIRS; 2.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR PIRSF; PIRSF001587; FGAM_synthase_II; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..725
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurL"
FT /id="PRO_0000100503"
FT ACT_SITE 41
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 66..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 83..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 303..305
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 430
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22232163"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22232163"
FT BINDING 485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 522..523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 525
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 620
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22232163"
FT HELIX 2..7
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:3VIU"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 95..112
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 116..127
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 132..152
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 172..182
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 331..347
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:3VIU"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 439..448
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 451..456
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 458..475
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 479..488
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 495..515
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 519..525
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 538..548
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 554..556
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 578..584
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 596..611
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 616..620
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 625..634
FT /evidence="ECO:0007829|PDB:3VIU"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 650..653
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 661..665
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 670..679
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 684..690
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 692..699
FT /evidence="ECO:0007829|PDB:3VIU"
FT STRAND 702..707
FT /evidence="ECO:0007829|PDB:3VIU"
FT HELIX 708..723
FT /evidence="ECO:0007829|PDB:3VIU"
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
