PUR4_XYLFT
ID PUR4_XYLFT Reviewed; 1322 AA.
AC Q87DN2;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-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=PD_0650;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(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; AE009442; AAO28521.1; -; Genomic_DNA.
DR RefSeq; WP_011097732.1; NC_004556.1.
DR AlphaFoldDB; Q87DN2; -.
DR SMR; Q87DN2; -.
DR EnsemblBacteria; AAO28521; AAO28521; PD_0650.
DR GeneID; 58016196; -.
DR KEGG; xft:PD_0650; -.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002516; 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..1322
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100427"
FT DOMAIN 1073..1322
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1166
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1287
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1289
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 300..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 702
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 703
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 742
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 746
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 915
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 917
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1322 AA; 143774 MW; CE3A7CCDB06AC65B CRC64;
MIVLKGASAL SPFRLARFES RLQTTVPELR IVGAWHCYLI QIKSGHTLDM SALHRILQAE
SVSELPQKHV VSRYVMPRLG THSPWSSKTT ELLHGADQPI ARIERGTRID LLGWSANAAT
CPAIAKQLYD PMTQSLLESE DEVKTLFNVP EPRPLERIAL IDLEHANTRL GLALTADEID
YLRTRYTELN RVPSDVELMM FAQANSEHCR HKIFNATWTI DDKEQPYSLF QMIKHTHQHT
PQYTLSAYAD NAAVIEGHPT TRYRPDPITG EYRHEAVLPG AFQIKVETHN HPTAIAPFPG
ASTGAGGEIR DEGATGRGGK PKAGLSGFSV SHLRIPTLPH PWETPRALNP RMASALDIML
EGPLGSAAFN NEFGRPNLLG YFRSFELSAS KTLTRAYDKP IMLAGGLGAI DRIHIKKLRL
QPGDVIIVLG GPAMLIGLGG GAASSVTSGT STEALDFASV QRDNPEMQRR CQEVIDHCVA
LGTNNPIRSF HDVGAGGLSN AIPELLHDSE VGGVIDLAKI PSDDPSLSPL ELWCNESQER
YVLGISAPHL QAFAAICSRE RCPFAAVGVA TATEQLIVGY GVTLPAALHV TEQQTPQRAN
RTETSPTPNT LVSPVREAFA IDLPMDVLFG KAPKMHRNTA HPPPPQWPTL DSTQLDLHHA
GLRVLAHPTV AAKNFLVTIG DRSIGGLTAR EQMIGPWQLP LADCAITLAG FSSYAGEAFA
IGERAPLALL NSAAAARMAV GEAITNLCAA PVESLSMVKL SANWMAAAEY PGEDALLYDA
VKAIGIELCP ALDISIPVGK DSLSMQSRWQ GDGATHTCIS PVSLVISAFT PVADARRQLT
PLLHHQTNSE LWLIALDGGK QRLGGSVLAQ VHADSAALPA FGGECPDLDT PETLRAFFAL
MNDARNAGLL LAYHDRSDGG AFAALCEMAF ASHLGLDITC DNRTEHLFPH LFNEELGAIV
QVADEHRTAF ADLVEHHGLT AYTQRIAHPT TAPSIRVMHN DQCLAQWTWE TLFDAWWSVT
HAIQRLRDNP ECADEEREIA RTFTAPGLKP TLSFDPAADV AMPFISTGIR PKVAILREQG
INGHIEMALC FERAGFHSVD IHMNDLITGR VHLDEFVGLA ACGGFSYGDV LGAGRGWATS
ILERTALRDQ FAAFFTRTDR FALGVCNGCQ MLSQLKSMIP GAEHWPRFVR NRSEQFEART
ALLEVIQSPS IFLSGMAGSR LPVAVAHGEG YAMFDTPADQ AAAHVALRYI NGHGQAATHY
PLNPNGSPNG ITGLTTTDGR ITILMPHPER TPRTINLSWC PNEWGEDAPW LRLFRNARAW
VG
