PUR4_PSEPK
ID PUR4_PSEPK Reviewed; 1299 AA.
AC Q88P16;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=PP_1037;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015451; AAN66662.1; -; Genomic_DNA.
DR RefSeq; NP_743198.1; NC_002947.4.
DR RefSeq; WP_010952214.1; NC_002947.4.
DR AlphaFoldDB; Q88P16; -.
DR SMR; Q88P16; -.
DR STRING; 160488.PP_1037; -.
DR EnsemblBacteria; AAN66662; AAN66662; PP_1037.
DR KEGG; ppu:PP_1037; -.
DR PATRIC; fig|160488.4.peg.1100; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR PhylomeDB; Q88P16; -.
DR BioCyc; PPUT160488:G1G01-1110-MON; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000556; 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..1299
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100414"
FT DOMAIN 1046..1299
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 301..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1139
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1264
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1266
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 1299 AA; 140819 MW; CE3C89D988AA7EA6 CRC64;
MLILRGAPAL SAFRHGKLLE QLSQKVPAVT GLYAEFAHFA DVDGELTADQ QQVLGRLLKY
GPSVPVQEPT GRLFLVVPRL GTISPWASKA SDIAHNCGLQ SIQRLERGIA YYVAGTLSDA
DAELIAAELH DRMTQRVLGQ LEQAADLFSH AQPKPMTSVD ILAGGRDALA KANIDLGLAL
AEDEIDYLVN AFQGLKRNPN DIELMMFAQA NSEHCRHKIF NASWDIDGQA QEKSLFGMIK
NTYQMHNEGV LSAYKDNASV IVGNVAGRFF PNPETRQYGA VQEPVHILMK VETHNHPTAI
APFSGASTGS GGEIRDEGAT GRGAKPKAGL TGFTVSNLRI PGFEQPWEQA YGKPERIVDA
LDIMIEGPLG GAAFNNEFGR PALTGYFRTF EQAINTPHGE EVRGYHKPIM LAGGMGNIRE
DHVQKGEITV GAKLIVLGGP AMLIGLGGGA ASSVATGASS ADLDFASVQR ENPEMERRCQ
EVIDRCWQLG DENPIAFIHD VGAGGISNAF PELVNDGGRG GRFELRNVPN DEPGMAPHEI
WSNESQERYV LAVSAVDFER FKAICERERC PFAVVGEATE EQHLTVSDSH FGNTPVDMPL
DVLLGKPPRM HRSVTREAEL GDDFDPSELD LDSAVQRVLN HPAVASKSFL ITIGDRTITG
LVARDQMVGP WQVPVADCAV TATSFDVYTG EAMAMGERTP LALLDAPASG RMAIGETLTN
LAASRIEKLS DIKLSANWMS AAGHPGEDAR LYDTVKAVGM ELCPELGITI PVGKDSMSMK
TKWSDEGVEK SVTSPMSLII TGFAPVTDIR KTLTPQLRMD KGETDLILID LGRGKNRMGA
SILAQTYGKI AAQAPDVDDA EDLKAFFAVI QGLNADGHLL AYHDRSDGGL VTTVLEMAFA
GHCGLDLQLD PLTDSKGEVP AILFNEELGA VIQVRQDATP DVLAQFSAAG LGEECVAVIG
KPVNNAEVTI SLNGEVLFDD DRRMLQRQWA ETSYQIQRLR DNADCADQEF DLLLEEDNPG
LSVKLGFDVN DDIAAPYIKK GVRPQVAILR EQGVNGQVEM AAAFDRAGFA AIDVHMSDIL
AGRVDFEAFK GLVACGGFSY GDVLGAGEGW AKSALFNARA RDAFQAFFER TDSFALGVCN
GCQMMSNLHE LIPGTEYWPH FVRNRSEQFE ARVAMVEVQK SNSIFLQGMA GSRMPIAIAH
GEGHAEFASE EALLEADVSG CVALRYVDNH GKVTEAYPAN PNGSPRGITG LTSRDGRVTI
MMPHPERVFR AVQNSWRPDE WQEDAALMRM FRNARVWVN
