ID   PUR4_SHEDO              Reviewed;        1293 AA.
AC   Q12PR7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   02-SEP-2026, entry version 107.
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};
GN   OrderedLocusNames=Sden_1273;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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=N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + L-
CC         glutamine + ATP + H2O = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC         ribosyl)acetamidine + L-glutamate + ADP + phosphate + H(+);
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; CP000302; ABE54559.1; -; Genomic_DNA.
DR   RefSeq; WP_011495718.1; NC_007954.1.
DR   AlphaFoldDB; Q12PR7; -.
DR   SMR; Q12PR7; -.
DR   STRING; 318161.Sden_1273; -.
DR   MEROPS; C56.972; -.
DR   KEGG; sdn:Sden_1273; -.
DR   eggNOG; COG0046; Bacteria.
DR   eggNOG; COG0047; Bacteria.
DR   HOGENOM; CLU_001031_0_2_6; -.
DR   OrthoDB; 9804441at2; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000001982; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   CDD; cd01740; GATase1_FGAR_AT; 1.
DR   CDD; cd02203; PurL_repeat1; 1.
DR   CDD; cd02204; PurL_repeat2; 1.
DR   FunFam; 1.10.8.750:FF:000002; Phosphoribosylformylglycinamidine synthase; 1.
DR   FunFam; 3.30.1330.10:FF:000002; Phosphoribosylformylglycinamidine synthase; 1.
DR   FunFam; 3.30.1330.10:FF:000005; Phosphoribosylformylglycinamidine synthase; 1.
DR   FunFam; 3.40.50.880:FF:000008; Phosphoribosylformylglycinamidine synthase; 1.
DR   FunFam; 3.90.650.10:FF:000002; Phosphoribosylformylglycinamidine synthase; 1.
DR   FunFam; 3.90.650.10:FF:000005; Phosphoribosylformylglycinamidine synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR   HAMAP; MF_00419; PurL_1; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR040707; FGAR-AT_N.
DR   InterPro; IPR055181; FGAR-AT_PurM_N-like.
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   NCBIfam; TIGR01735; FGAM_synt; 1.
DR   NCBIfam; NF003672; PRK05297.1; 1.
DR   PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   Pfam; PF02769; AIRS_C; 2.
DR   Pfam; PF18072; FGAR-AT_linker; 1.
DR   Pfam; PF18076; FGAR-AT_N; 1.
DR   Pfam; PF22689; FGAR-AT_PurM_N-like; 1.
DR   Pfam; PF13507; GATase_5; 1.
DR   SMART; SM01211; GATase_5; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR   SUPFAM; SSF82697; PurS-like; 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..1293
FT                   /note="Phosphoribosylformylglycinamidine synthase"
FT                   /id="PRO_0000264593"
FT   DOMAIN          1040..1293
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1133
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1258
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1260
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         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   1293 AA;  140347 MW;  A916126B88D3D748 CRC64;
     MEIIRGAPAL SAFRVQQLMK ACDAAAIPVR HIYAEFMHFA HLTNALNDTQ TLQLASILTY
     GPAIEAHTPK GQLYLVTPRP GTISPWSSKA TDIAHNCGLS QIKRLERGIA YYVEADTLDA
     SQQKALQALL YDRMVEVIFD DMAAAETLFD RTEPKALASV NVLGEGRRAL EVANSRLGLA
     LAEDEIDYLV DNFVRLKRNP NDIELMMFAQ ANSEHCRHKI FNADWTIDGV VQDKSLFKMI
     KNTYAVTPDN VLSAYKDNAA VMTGSVAGRF FPDETGVYAY HVEPCHILMK VETHNHPTAI
     SPYAGAATGS GGEIRDEGAT GRGSKPKAGL VGFSVSNLNI PGFIQPWEAQ YGKPERIVTP
     LEIMLEGPLG GAAFNNEFGR PALVGYFRTY EQEVSSHNGV EVRGYHKPIM LAGGLGNIRE
     DHVQKGEITV GAKLIVLGGP AMNIGLGGGA ASSMASGQSS EDLDFASVQR ENPEMERRCQ
     EVIDRCWQLG DDNPIQFIHD VGAGGLSNAF PELVNDADRG GRFNLRNVPS DEPGMSPLEI
     WCNESQERYV LSVAPENLAR FEQICLRERA PFAVVGEATS EQHLTLADSH FNNKPIDLPL
     EVLLGKAPKM SRDVVSKKAL SPALDESQIT VDEAVTRILS LPTVADKSFL ITIGDRSVTG
     LVNRDQMVGP WQVPVADCAV TAASFDTYAG EAMSIGERTP LALLDFGASA RMAVAESIMN
     IAGTDIGSFK RIKLSANWMS AAGHPGEDAG LYEAVKAVGE ELCPQLEITI PVGKDSMSMK
     TAWEDNGVHK SVTSPMSLVI TAFGVVQDIR NTVTPELRSD KGDTALLLLD LSHGKTRLGG
     SCLAQVFSSL GDVAPDLDDS TTLKGFFEVM QTLVADQSIL AYHDRSDGGL FTTVTEMAFA
     GNTGAEIDLS ALQGSDLARL FNEELGAVIQ VSQAQAEAIT AQFIAAGVAC HAIGGLTEHN
     KLVVKDGSRV VFQQQRSELR RLWSQTSYKM QALRDNPDCA LEEFSLKQSE TDPGLTVKLN
     FDPSQDVAAP YILKGIAPKM AILREQGVNS HVEMAAAFDR AGFESRDVHM SDILSGRISL
     DEFQGLVACG GFSYGDVLGA GEGWAKSILF NQRARDEFSR FFERDLSFAL GVCNGCQMLS
     NLKEIIPGSE HWPRFVRNRS ERFEARVSLV EVQQSPSLFF EGMAGSRMPI AVSHGEGLAE
     FASMQAMTAA ESTGTVALRY VTGTGEIATQ YPQNPNGSPN GLSGICSTDG KVTIMMPHPE
     RVFRTVANSW HPDNWGEDSP WMRMFRNARV KLG
//