PUR4_PSEU2
ID PUR4_PSEU2 Reviewed; 1298 AA.
AC Q4ZX02;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Psyr_1269;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY36320.1; -; Genomic_DNA.
DR RefSeq; WP_011266924.1; NC_007005.1.
DR RefSeq; YP_234358.1; NC_007005.1.
DR AlphaFoldDB; Q4ZX02; -.
DR SMR; Q4ZX02; -.
DR STRING; 205918.Psyr_1269; -.
DR PRIDE; Q4ZX02; -.
DR EnsemblBacteria; AAY36320; AAY36320; Psyr_1269.
DR KEGG; psb:Psyr_1269; -.
DR PATRIC; fig|205918.7.peg.1301; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000426; 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_0000264590"
FT DOMAIN 1045..1298
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 303..327
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; 140906 MW; 19042BEE9302342E CRC64;
MLILRGAPAL SAFRHSKLLE QLKQKVSAVS GLYAEFAHFA DVNDVLTSEE QQVLDRLLKY
GPSVPVQEPS GRLFLVLPRF GTISPWSSKA SDIARNCGLS KIQRLERGIA FYVEGQFSET
EAQAIADSLH DRMTQLVLGD LEQAANLFSH AQPKPLTAVD ILGGGRAALE KANVELGLAL
AEDEIDYLIT SFNGLGRNPH DIELMMFAQA NSEHCRHKIF NASWDIDGQS QEKSLFGMIK
NTYQMHSEGV LSAYKDNASV IVGNVAGRFF PDPETRQYGA VQEPVHILMK VETHNHPTAI
APFPGAATGS GGEIRDEGAT GRGAKPKAGL TGFTVSNLQI PGFVQPWEVP YGKPERIVTA
LDIMIEGPLG GAAFNNEFGR PALTGYFRTF EQSITTPHGD EVRGYHKPIM LAGGMGNIRE
DHVQKGEITV GSKLIVLGGP AMLIGLGGGA ASSMATGTSS ADLDFASVQR ENPEMERRCQ
EVIDRCWQLG DRNPISFIHD VGAGGLSNAF PELVNDGDRG GRFELRNVPN DEPGMAPLEI
WSNESQERYV LAVGVEDFER FKAICERERC PFAVVGEATA EPQLTVTDSH FGNSPVDMPL
EVLLGKAPRM HRSVAREEEI GDDFDPSTLD IEESVQRVLR HPAVASKSFL ITIGDRSITG
LVARDQMVGP WQVPVADCAV TATSFDVNTG EAMAMGERTP LALLDAPASG RMAIGETLTN
IAASLIEKLS DIKLSANWMS AAGHPGEDAR LYDTVKAVGM ELCPELGITI PVGKDSMSMK
TRWSDEGTEK SVTSPLSLIV TGFAPVVDIR QTLTPELRMD KGITDLILID LGRGQNRMGA
SILAQTHGKL GRVAPDVDDA EDLKAFFAVI QGLNSDGHIL SYHDRSDGGL LVSTLEMAFA
GHCGLNLHLD GVADNVSELS AILFNEELGA VIQVRQDATP LVLAQFSAAG LEDCVAVIGQ
PINNDEVSIS FHGEPVFSGQ RRLLQRQWAE TSYQIQRLRD NAECADQEFD ALLEEDNPGL
TVKLGFDVND DIAAPYIKTG VRPQVAVLRE QGVNGQVEMA AAFDRAGFNA IDVHMSDILA
GRVDLNDFKG MVACGGFSYG DVLGAGEGWA KSALFNSRAR DAFQGFFERS DSFTLGVCNG
CQMLSNLHEL IPGSEFWPHF VRNRSEQFEA RVAMVQVQES ASIFLQGMAG SRMPIAIAHG
EGHAEFRNDD ALLEADVSGT VALRFVDNHG KVTETYPANP NGSPRGIGGM TTLDGRVTIM
MPHPERVFRA VQNSWRPEDW NEDGAWMRMF RNARAWVN
