PUR4_ECOLI
ID PUR4_ECOLI Reviewed; 1295 AA.
AC P15254; P78097; Q2MAH3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 189.
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}; Synonyms=purI;
GN OrderedLocusNames=b2557, JW2541;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=2659070; DOI=10.1021/bi00432a017;
RA Schendel F.J., Mueller E., Stubbe J., Shiau A., Smith J.M.;
RT "Formylglycinamide ribonucleotide synthetase from Escherichia coli:
RT cloning, sequencing, overproduction, isolation, and characterization.";
RL Biochemistry 28:2459-2471(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2531746; DOI=10.1016/s0021-9258(19)30071-7;
RA Sampei G., Mizobuchi K.;
RT "The organization of the purL gene encoding 5'-
RT phosphoribosylformylglycinamide amidotransferase of Escherichia coli.";
RL J. Biol. Chem. 264:21230-21238(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP SEQUENCE REVISION TO 847.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(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, ECO:0000269|PubMed:2659070}.
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, ECO:0000269|PubMed:2659070};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=64 uM for glutamine (at pH 7.25 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:2659070};
CC KM=51 uM for ATP (at pH 7.25 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:2659070};
CC KM=30 uM for FGAR (formylglycinamide ribonucleotide at pH 7.25 and 37
CC degrees Celsius) {ECO:0000269|PubMed:2659070};
CC pH dependence:
CC Optimum pH is 7.2 with only 50% of this activity retains at pH 6.2 or
CC 8.0. {ECO:0000269|PubMed:2659070};
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 ECO:0000269|PubMed:2659070}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419,
CC ECO:0000269|PubMed:2659070}.
CC -!- PTM: Both N-terminus methionine truncation and retention have been
CC observed for this protein. {ECO:0000269|PubMed:2659070}.
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; M19501; AAA24456.1; -; Genomic_DNA.
DR EMBL; U36841; AAA79819.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48143.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76733.1; -; Genomic_DNA.
DR PIR; D65033; SYECPG.
DR RefSeq; WP_000970102.1; NZ_LN832404.1.
DR RefSeq; YP_026170.1; NC_000913.3.
DR AlphaFoldDB; P15254; -.
DR SMR; P15254; -.
DR BioGRID; 4259206; 75.
DR DIP; DIP-10614N; -.
DR IntAct; P15254; 14.
DR STRING; 511145.b2557; -.
DR MEROPS; C56.972; -.
DR jPOST; P15254; -.
DR PaxDb; P15254; -.
DR PRIDE; P15254; -.
DR EnsemblBacteria; AAT48143; AAT48143; b2557.
DR EnsemblBacteria; BAE76733; BAE76733; BAE76733.
DR GeneID; 947032; -.
DR KEGG; ecj:JW2541; -.
DR KEGG; eco:b2557; -.
DR PATRIC; fig|1411691.4.peg.4177; -.
DR EchoBASE; EB0790; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR InParanoid; P15254; -.
DR OMA; LSANWMW; -.
DR PhylomeDB; P15254; -.
DR BioCyc; EcoCyc:FGAMSYN-MON; -.
DR BioCyc; MetaCyc:FGAMSYN-MON; -.
DR UniPathway; UPA00074; UER00128.
DR PRO; PR:P15254; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoliWiki.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoliWiki.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IDA:EcoCyc.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IC:EcoliWiki.
DR GO; GO:0006541; P:glutamine metabolic process; IDA:EcoliWiki.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing;
KW Glutamine amidotransferase; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..1295
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100406"
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; 141403 MW; 30943AA218D758FE CRC64;
MMEILRGSPA LSAFRINKLL ARFQAARLPV HNIYAEYVHF 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 RGGKFELREI 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 EREMTSPLSL VISAFARVED VRHTITPQLS TEDNALLLID LGKGNNALGA
TALAQVYRQL GDKPADVRDV AQLKGFYDAI QALVAQRKLL AYHDRSDGGL LVTLAEMAFA
GHCGIDADIA TLGDDRLAAL FNEELGAVIQ VRAADREAVE SVLAQHGLAD CVHYVGQAVS
GDRFVITANG QTVFSESRTT LRVWWAETTW QMQRLRDNPE CADQEHQAKS NDADPGLNVK
LSFDINEDVA APYIATGARP KVAVLREQGV NSHVEMAAAF HRAGFDAIDV HMSDLLTGRT
GLEDFHALVA CGGFSYGDVL GAGEGWAKSI LFNDRVRDEF ATFFHRPQTL ALGVCNGCQM
MSNLRELIPG SELWPRFVRN TSDRFEARFS LVEVTQSPSL LLQGMVGSQM PIAVSHGEGR
VEVRDAAHLA ALESKGLVAL RYVDNFGKVT ETYPANPNGS PNGITAVTTE SGRVTIMMPH
PERVFRTVSN SWHPENWGED GPWMRIFRNA RKQLG
