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PURL_METS5
ID   PURL_METS5              Reviewed;         702 AA.
AC   A4YI68;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Msed_1980;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP96120.1; -; Genomic_DNA.
DR   RefSeq; WP_012021907.1; NC_009440.1.
DR   AlphaFoldDB; A4YI68; -.
DR   SMR; A4YI68; -.
DR   STRING; 399549.Msed_1980; -.
DR   EnsemblBacteria; ABP96120; ABP96120; Msed_1980.
DR   GeneID; 5103367; -.
DR   GeneID; 59456886; -.
DR   KEGG; mse:Msed_1980; -.
DR   eggNOG; arCOG00641; Archaea.
DR   HOGENOM; CLU_003100_0_1_2; -.
DR   OMA; FIEPYQG; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000000242; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..702
FT                   /note="Phosphoribosylformylglycinamidine synthase subunit
FT                   PurL"
FT                   /id="PRO_1000072299"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   ACT_SITE        84
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         82
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         83..86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         106
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         251
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         293..295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         468
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         505
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         508
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
SQ   SEQUENCE   702 AA;  75625 MW;  18F3D83EBF6E3F1E CRC64;
     MILTLSKTEM EVVRRVLGRE PKEAEWKLVD ALWSEHCSYK SSKVFLRSLP STGPNVIMSV
     EDWQDAGAVD VGDGLALVLK VESHNHPSAI DPFNGAATGV GGILRDIISK GAKPIALLDM
     IRVGKLDDKG KWLLKNIISG IGFYGNSVGV PVVGGELSFD ETYNDNPLVD VACAGIVSKD
     SIVPSVVREP GLRLVLAGFT GLDGLGGASF ASRKLSGMDE IGAVQIADPF AGKIIIDVTL
     EIAKEVEAIK DLGGGGLAVA VTEMANGLGA VVNLERVPLR FEYLSPEDII ISETQERMLF
     AVKPEKVESV CAKFREYNYP CEDIGEITAE PKVRFLYNGE PVAELPSDLL LSPPLNVWPA
     ERKPRKREPE REVALGEALR AVLTHPDLVS KEWAYSQFDY EVGTSTVVKP GQGDSAVVEL
     PNGKYLALKG DANQDLCAED AYECGKAIVA EAYRNLATVG ARGIALVDHL QFGDPRKPHV
     YQDFIDAVRG ISEASKFFSI PVVGGKVSFH NEDKNGNPIK PTPLVVMAGL VEGKLARNRV
     EEGDLVLIGE TRNELAGTLF SRIFGGGGEV AKTRLMEDLI ASNLVIKGIN EGKITWNKDV
     SKGGLAGALL PILAKGFSVR ISSSQVIGTS NLLGKMFSES GGRFLVLTSD PQWFMYQAGR
     MGIQALAIGK VTKDGSKLVL DYETFPMDSI VENYYSFLEG SL
 
 
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