PUR4_ECOL5
ID PUR4_ECOL5 Reviewed; 1295 AA.
AC Q0TET1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 111.
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=ECP_2559;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG70548.1; -; Genomic_DNA.
DR RefSeq; WP_001298398.1; NC_008253.1.
DR AlphaFoldDB; Q0TET1; -.
DR SMR; Q0TET1; -.
DR STRING; 362663.ECP_2559; -.
DR MEROPS; C56.972; -.
DR EnsemblBacteria; ABG70548; ABG70548; ECP_2559.
DR KEGG; ecp:ECP_2559; -.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000009182; 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..1295
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264574"
FT DOMAIN 1042..1295
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1135
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1260
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1262
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 307..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 678
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 718
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 722
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 1295 AA; 141176 MW; 826B090BAEAC6A15 CRC64;
MMEILRGSPA LSAFRINKLL ARFQAARLPV HTIYAEYVHF ADLNAPLNDD EHAQLERLLK
YGPALASHAP QGKLLLVTPR PGTISPWSSK ATDIAHNCGL QQVNRLERGV AYYIEAGTLT
NEQWQQVTAE LHDRMMETVF FALDDAEQLF AHHQPTPVTS VDLLGQGRQA LIDANLRLGL
ALAEDEIDYL QDAFTKLGRN PNDIELYMFA QANSEHCRHK IFNADWVIDG EQQPKSLFKM
IKNTFETTPD HVLSAYKDNA AVMEGSEVGR YFADHETGRY DFHQEPAHIL MKVETHNHPT
AISPWPGAAT GSGGEIRDEG ATGRGAKPKA GLVGFSVSNL RIPGFEQPWE EDFGKPERIV
TALDIMTEGP LGGAAFNNEF GRPALNGYFR TYEEKVNSHN GEELRGYHKP IMLAGGIGNI
RADHVQKGEI NVGAKLVVLG GPAMNIGLGG GAASSMASGQ SDADLDFASV QRDNPEMERR
CQEVIDRCWQ LGDANPILFI HDVGAGGLSN AMPELVSDGG RGGKFELRDI LSDEPGMSPL
EIWCNESQER YVLAVAADQL PLFDELCKRE RAPYAVIGEA TEELHLSLHD RHFDNQPIDL
PLDVLLGKTP KMTRDVQTLK AKGDALAREG ITIADAVKRV LHLPTVAEKT FLVTIGDRSV
TGMVARDQMV GPWQVPVANC AVTTASLDSY YGEAMAIGER APVALLDFAA SARLAVGEAL
TNIAATQIGD IKRIKLSANW MAAAGHPGED AGLYEAVKAV GEELCPALGL TIPVGKDSMS
MKTRWQEGNE ECEMTSPLSL VISAFARVED VRHTITPQLS TEDNALLLID LGKGNNALGA
TALAQVYRQL GDKPADVRDV AQLKGFYDAI QALVAQRKLL AYHDRSDGGL LVTLAEMAFA
GHCGIDADIA TLGDDRLAAL FSEELGAVIQ VRAADREAVE AVLAQHGLAD CVHYVGQAVS
GDRFVITANG QTVFSESRTT LRVWWAETTW QMQRLRDNPE CADQEHQAKS NDADPGLNVK
LSFDINEDVA APFIATGARP KVAVLREQGV NSHVEMAAAF HRAGFDAIDV HMSDLLAGRT
GLEGFHALVA CGGFSYGDVL GAGEGWAKSI LFNDRVRDEF ATFFHRPQTL ALGVCNGCQM
MSNLRELIPG SELWPRFVRN TSDRFEARFS LVEVTQSPSL LLQGMVGSQM PIAVSHGEGR
VEVRDAAHLA ALESKGLVAL RYVDNFGKVT ETYPANPNGS PNGITAVTTE SGRVTIMMPH
PERVFRTVSN SWHPENWGED GPWMRIFRNA RKQLG
