PUR4_PSEAE
ID PUR4_PSEAE Reviewed; 1298 AA.
AC Q9HXN2;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=PA3763;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG07150.1; -; Genomic_DNA.
DR PIR; B83175; B83175.
DR RefSeq; NP_252452.1; NC_002516.2.
DR RefSeq; WP_003113821.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HXN2; -.
DR SMR; Q9HXN2; -.
DR STRING; 287.DR97_4112; -.
DR PaxDb; Q9HXN2; -.
DR PRIDE; Q9HXN2; -.
DR EnsemblBacteria; AAG07150; AAG07150; PA3763.
DR GeneID; 879752; -.
DR KEGG; pae:PA3763; -.
DR PATRIC; fig|208964.12.peg.3938; -.
DR PseudoCAP; PA3763; -.
DR HOGENOM; CLU_001031_0_2_6; -.
DR InParanoid; Q9HXN2; -.
DR OMA; LSANWMW; -.
DR PhylomeDB; Q9HXN2; -.
DR BioCyc; PAER208964:G1FZ6-3834-MON; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002438; 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..1298
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100413"
FT DOMAIN 1045..1298
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 298..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1138
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1263
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1265
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 305..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 384..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 677
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 716
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 884
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1298 AA; 140647 MW; 95BBE47CCA4FE8D1 CRC64;
MLILRGAPAL SAFRHGKLLE QLTQHVPAVT GLYAEFAHFA DVTGALTADE EQVLARLLKY
GPSVPVQEPS GRLFLVVPRF GTISPWSSKA SDIARNCGLA KIDRLERGIA YYVQGELSES
DAQQVAARLH DRMTQLVLDR LEGAAELFSH AQPRPLTAVD VLGGGRAALE KANVELGLAL
AEDEIDYLLK SFGELGRNPH DVELMMFAQA NSEHCRHKIF NASWDIDGQA QDKSLFGMIK
NTYEMNREGV LSAYKDNAAV IVGHVAGRFF PDPQTREYAA SREPVQILMK VETHNHPTAI
APFPGASTGS GGEIRDEGAT GRGAKPKAGL TGFTVSNLQI PGFEQPWEVP YGKPERIVTA
LDIMVEGPLG GAAFNNEFGR PALTGYFRTF EQKIATPHGE EVRGYHKPIM LAGGMGNIRD
EHVQKGEISV GAKLIVLGGP AMLIGLGGGA ASSMATGASS ADLDFASVQR DNPEMERRCQ
EVIDRCWQLG ERNPISFIHD VGAGGLSNAL PELINDGGRG GRFELRAVPN DEPGMSPLEI
WCNESQERYV LSVDAADFET FKAICERERC PFAVVGEAIE QRQLTVADSH FDNKPVDMPL
EVLLGKAPRM HRAVTREAEL GDDFDAAGLE LQESVERVLR HPAVASKSFL ITIGDRTITG
LVARDQMVGP WQVPVADCAV TATSFDVYTG EAMAMGERTP LALLDAPASG RMAIGETVTN
LAAARVGKLS DIKLSANWMA AAGHPGEDAR LYDTVKAVGM ELCPELGITI PVGKDSMSMK
TRWQDNGEDK SVTSPVSLIV TGFAPVADVR QSLTPQLRLD KGETDLILID LGRGKNRLGG
SILAQVHGKL GRAVPDVDDA EDLKAFFAVI QGLNADGHIL AYHDRSDGGL ITSVLEMAFA
GHCGVELNLD ALADSREELA AVLFSEELGA VIQVREGATP EVLAQFSAAG LDDCVAVIGQ
PVNGYEINLN YNGETVYSAQ RRILQRIWSE TSYQIQRLRD NADCAEQEFD ALLDEDNPGL
SIKLSYDVND DIAAPYIKKG VRPKVAILRE QGVNGQVEMA AAFDRAGFAA IDVHMSDILA
GRVDLDAFKG LVACGGFSYG DVLGAGEGWA KSILFNARAR DGFQAFFARK DSFALGVCNG
CQMMSNLHEL IPGTEFWPHF VRNRSEQFEA RVAMVQVQES SSIFLQGMAG SRLPIAIAHG
EGHAEFESEE ALLEADLSGC VSLRFVDNHG KVTEAYPANP NGSPRGITGL SSRDGRVTIM
MPHPERVFRA VQNSWRPDDW QEDGGWLRMF RNARVWVD
