PUR4_RALSO
ID PUR4_RALSO Reviewed; 1369 AA.
AC Q8XYN6;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAMS {ECO:0000255|HAMAP-Rule:MF_00419};
DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00419};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAR amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAR-AT {ECO:0000255|HAMAP-Rule:MF_00419};
GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00419}; OrderedLocusNames=RSc1722;
GN ORFNames=RS02912;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the
CC purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC formylglycinamidine ribonucleotide (FGAM) and glutamate.
CC {ECO:0000255|HAMAP-Rule:MF_00419}.
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_00419};
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_00419}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000255|HAMAP-Rule:MF_00419}.
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DR EMBL; AL646052; CAD15424.1; -; Genomic_DNA.
DR RefSeq; WP_011001661.1; NC_003295.1.
DR AlphaFoldDB; Q8XYN6; -.
DR SMR; Q8XYN6; -.
DR STRING; 267608.RSc1722; -.
DR EnsemblBacteria; CAD15424; CAD15424; RSc1722.
DR GeneID; 60501253; -.
DR KEGG; rso:RSc1722; -.
DR PATRIC; fig|267608.8.peg.1767; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_4; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; -; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_sf.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR SUPFAM; SSF82697; SSF82697; 1.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..1369
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100416"
FT DOMAIN 1116..1369
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 321..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1209
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1330
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1332
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 330..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 722
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 761
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 765
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 934
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 936
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1369 AA; 146481 MW; FAB0B960D77C6A1F CRC64;
MAHFSCFPGA LALSAFRQQR LLSTLKRIDP EIDAVSAQYL HFVAADAPLS ADDAARVQAL
LTYGSPASAE TEGDRFVVIP RFGTISPWAS KATEIARHCA LPQIHRIERG VEFTVTCKKG
LLRGLTGGRK QLDEATRAAV AAHLHDRMTE IVVATREAGY GLFDVLPAKA LRFVDLGSGD
AAAGRGALEA ANTEMGLALS DDEIDYLVDA YRKLGRNPTD VELMMFAQAN SEHCRHKIFN
ADWTIDGETQ DKSLFAMIRN THQLAPQGTV VAYSDNAAVM EGGMAERWFP HAGTDGETGV
PQYGRREALT HTLMKVETHN HPTAISPFPG ASTGAGGEIR DEGATGRGAK PKAGLTGFTV
SNLLLPEAVQ SWENARDTAQ PAAQRNPGDT APGPVGKPDR IASPLQIMIE GPIGGAAFNN
EFGRPNLGGY FRVYEQNVGG TVRGYHKPIM IAGGIGNIDA GHTHKHGLPA GTLLVQLGGP
GMRIGMGGGA ASSMATGTNT ADLDFDSVQR GNPEMQRRAQ EVINACWALG EDNPILSIHD
VGAGGISNAF PELVDGADRG ARFDLRQVHL EESGLSPAEI WCNESQERYT LAIAPGDFPR
FQAMCERERA PFSVVGFATE EQQLQVVDGD APADAVEHFP VNMPMDVLLG KPPRMHRDVR
RVAQALPEVD VTGLDLETVA RDVLRHPTVA SKSFLITIGD RTVGGLNTRD QMVGPWQVPV
ADVAVTTLDY KGYAGEAMTM GERTPLAVID APASGRMAIG EAITNIAAAP IASLAQLKLS
ANWMAACGVD GEDARLYDTV KAVGMELCPA LGISIPVGKD SLSMRTKWDD AGEAKEVVAP
VSLIVSAFAP VTDVRKTLTP QLKPVASAGE AADTTLIVID LGHGKHRLGG SILAQVTQQI
GNSVPDVGDA EDLKRFFAAI QQLNAAGMLL AYHDRSDGGL WATVCEMAFA GHCGVSINVD
MLTLDGAHAS DYGDAKNWAQ QVSGRRADMT LRALFAEELG AVIQVPAAQR DAVFAVLREH
GLAACSHVIG APNASGQIEI WRDAKKVFSA PRIELQRAWT DVSWRIASLR DNPECTQSEY
DRLLDAEDPG ISPNLTFDLA EDVAAPFIAT GARPRMAILR EQGVNSQVEM AYAMDKAGFD
AYDVHMSDLL AGRTRLADFK GFVACGGFSY GDVLGAGEGW AKTILFNGML AEQFAAFFNR
ADSIALGVCN GCQMMANLAP IIPGAGAWPK FTRNQSEQYE GRLVTVQVEA SPSIFYAGME
GSRIPIVVAH GEGYADFSQQ GDIGKVAVGL RYVDNRGEVT QTYPLNPNGS PQGIASVTTH
DGRFTVLMPH PERVFRAVQM SWHPKDWAAA GDGSSPWMRM FRNARKQMG
