PUR4_PSESM
ID PUR4_PSESM Reviewed; 1298 AA.
AC Q886W6;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=PSPTO_1459;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO54980.1; -; Genomic_DNA.
DR RefSeq; NP_791285.1; NC_004578.1.
DR RefSeq; WP_011103562.1; NC_004578.1.
DR AlphaFoldDB; Q886W6; -.
DR SMR; Q886W6; -.
DR STRING; 223283.PSPTO_1459; -.
DR EnsemblBacteria; AAO54980; AAO54980; PSPTO_1459.
DR GeneID; 1183096; -.
DR KEGG; pst:PSPTO_1459; -.
DR PATRIC; fig|223283.9.peg.1481; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 26038at2; -.
DR PhylomeDB; Q886W6; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002515; 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; ISS:JCVI.
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 GO; GO:0009152; P:purine ribonucleotide biosynthetic process; ISS:JCVI.
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_0000100415"
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; 140647 MW; 021B429EC6402AB6 CRC64;
MLILRGAPAL SAFRHSKLLE QLKQKVSAVS GLYAEFAHFA DVNDVLTGEE QQVLDRLLKY
GPSVPVQEPA GRLFLVLPRF GTISPWSSKA SDIARNCGLT KIQRIERGIA FYVEGQFSDA
DAQAIADSLH DRMTQLVLGD HAQAAGLFSH AEPKPLTAVD ILGGGRAALE KANVELGLAL
AEDEIDYLIT SFNGLGRNPH DIELMMFAQA NSEHCRHKIF NASWDIDGQS QEKSLFGMIK
NTYEMHSEGV LSAYKDNASV IVGSVAGRFF PDPDTRQYGA VQEPVHILMK VETHNHPTAI
APFPGAATGS GGEIRDEGAT GRGAKPKAGL TGFTVSNLQI PGFVQPWEVP YGKPERIVTA
LDIMIEGPLG GAAFNNEFGR PALTGYFRTF EQSITTPHGD EVRGYHKPIM LAGGMGNIRE
DHVQKAEITV GSKLIVLGGP AMLIGLGGGA ASSMATGTSS ADLDFASVQR ENPEMERRCQ
EVIDRCWQLG DRNPISFIHD VGAGGLSNAF PELVNDGDRG GRFELRNVPN DEPGMAPLEI
WSNESQERYV LAVGVADYER FKAICERERC PFAVVGEATA EPQLTVTDSH FGNSPVDMPL
EVLLGKAPRM HRSVAREAEI GDDFDPSTLD IEESVQRVLR HPAVASKSFL ITIGDRSITG
LVARDQMVGP WQVPVADCAV TATSFDVNTG EAMAMGERTP LALLDAPASG RMAIGETLTN
IAASRIEKLS DIKLSANWMS AAGHPGEDAR LYDTVKAVGM ELCPELGITI PVGKDSMSMK
TRWSDEGTEK SVTSPLSLIV TGFAPVVDIR KTLTPELRMD KGITDLILID LGRGQNRMGA
SILAQTHGKL GRVAPDVDDA EDLKAFFAVI QGLNSDGHIL SYHDRSDGGL LVSTLEMAFA
GHCGLNLHLD GLADNVSELS AILFNEELGA VIQVRQDATP LVLAQFSAAG LEDCVAVIGQ
PINNDEVSIS FLGEPVFSGQ RRLLQRQWAE TSYQIQRLRD NAECADQEFD ALLEEDNPGL
TVKLGFDVNE DIAAPYIKTG VRPQVAVLRE QGVNGQVEMA AAFDRAGFNA IDVHMSDILA
GRVDLNDFKG MVACGGFSYG DVLGAGEGWA KSALFNSRAR DAFQGFFERS DSFTLGVCNG
CQMLSNLHEL IPGSEFWPHF VRNRSEQFEA RVAMVQVQES ASIFLQGMAG SRMPIAIAHG
EGHAEFRNDD ALLEADVSGT VALRFVDNHG KVTESYPANP NGSPRGIGGM TTLDGRVTIM
MPHPERVFRA VQNSWRPEDW NEDAAWMRMF RNARAWVN
