PUR4_PSEPF
ID PUR4_PSEPF Reviewed; 1298 AA.
AC Q3KHL4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=Pfl01_0999;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA72742.1; -; Genomic_DNA.
DR RefSeq; WP_011332594.1; NC_007492.2.
DR AlphaFoldDB; Q3KHL4; -.
DR SMR; Q3KHL4; -.
DR STRING; 205922.Pfl01_0999; -.
DR MEROPS; C56.972; -.
DR PRIDE; Q3KHL4; -.
DR EnsemblBacteria; ABA72742; ABA72742; Pfl01_0999.
DR KEGG; pfo:Pfl01_0999; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002704; 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.
FT CHAIN 1..1298
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264588"
FT DOMAIN 1045..1298
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 301..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; 140904 MW; 85DD6C14A2A2D090 CRC64;
MLILRGAPAL SAFRHSKLLE QLSQKVPAVS GLYAEFAHFA EVTGVLTGDE QQVLARLLKY
GPSVPVQEPT GRLFLVLPRF GTISPWSSKA SDIARNCGLS KIQRLERGIA FYVAGQFSET
EAQQIADVLH DRMTQIVLAN LEQAAGLFSH AEPKPLTAID ILGGGRAALE KANVELGLAL
AEDEIDYLVN AFNGLKRNPH DIELMMFAQA NSEHCRHKIF NASWDIDGES QEKSLFGMIK
NTYQMHSEGV LSAYKDNASV IVGNVAGRFF PDPETRQYGA VQEPVHILMK VETHNHPTAI
APFPGASTGS GGEIRDEGAT GRGAKPKAGL TGFTVSNLQI PGFEQPWEVP YGKPERIVNA
LDIMIEGPLG GAAFNNEFGR PALTGYFRTF EQSITTPHGD EVRGYHKPIM LAGGMGNIRE
EHVKKGEIVV GSKLVVLGGP AMLIGLGGGA ASSMATGTSS ADLDFASVQR ENPEMERRCQ
EVIDRCWQLG DKNPISFIHD VGAGGLSNAF PELVNDGDRG GRFELRNIPN DEPGMAPHEI
WSNESQERYV LAVGPADFER FKAICERERC PFAVVGEATA EPQLTVTDSH FGNNPVDMPL
EVLLGKAPRM HRSVVREAEL GDDFDPSNLD IGESIERVLH HPAVASKSFL ITIGDRTITG
LVARDQMVGP WQVPVADVAV TATSFDVYTG EAMAMGERTP LALLDAPASG RMAIGETITN
IAASRINKLS DIKLSANWMS AAGHPGEDAR LYDTVKAVGM ELCPELGITI PVGKDSMSMA
TRWNDNGEDK TVTSPMSLIV TGFAPVADIR QTLTPELRMD KGTTDLILID LGRGQNRMGA
SILAQVHGKL GKQAPDVDDA EDLKAFFAVI QGLNADGHLL AYHDRSDGGL LTSVMEMAFA
GHCGLSLNLD SVAESSAEIA AILFNEELGA VIQVRQDATP DILAQFSAAG LGDCVSVIGQ
PINNGQINIT FNGDTVFEGQ RRLLQRQWAE TSYQIQRLRD NADCAEQEFD ALLEEDNPGL
SVKLSYDVNQ DIAAPYIKKG IRPQVAVLRE QGVNGQVEMA AAFDRAGFNA IDVHMSDILA
GRVDLNEFKG LVACGGFSYG DVLGAGEGWA KSALFNSRAR DAFQGFFERN DSFTLGVCNG
CQMMSNLHEL IPGSEFWPHF VRNRSEQFEA RVAMVQVQES NSIFLQGMAG SRMPIAIAHG
EGHAEFESEE ALLEADLSGC VAMRFVDNHG KVTEAYPANP NGSPRGITGL TSRDGRVTIM
MPHPERVFRA VQNSWRSEDW NEDAPWMRMF RNARVWVN
