ID   PUR4_XANCP              Reviewed;        1348 AA.
AC   Q8PCQ7;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   02-SEP-2026, entry version 138.
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=XCC0656;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(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=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; AE008922; AAM39972.1; -; Genomic_DNA.
DR   RefSeq; WP_011035897.1; NC_003902.1.
DR   AlphaFoldDB; Q8PCQ7; -.
DR   SMR; Q8PCQ7; -.
DR   STRING; 190485.XCC0656; -.
DR   EnsemblBacteria; AAM39972; AAM39972; XCC0656.
DR   KEGG; xcc:XCC0656; -.
DR   PATRIC; fig|190485.4.peg.719; -.
DR   eggNOG; COG0046; Bacteria.
DR   eggNOG; COG0047; Bacteria.
DR   HOGENOM; CLU_001031_0_2_6; -.
DR   OrthoDB; 9804441at2; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000001010; 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; IBA:GO_Central.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR   CDD; cd01740; GATase1_FGAR_AT; 1.
DR   CDD; cd02203; PurL_repeat1; 1.
DR   CDD; cd02204; PurL_repeat2; 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:000024; 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..1348
FT                   /note="Phosphoribosylformylglycinamidine synthase"
FT                   /id="PRO_0000100425"
FT   DOMAIN          1099..1348
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1192
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1313
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1315
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         701
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         702
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         741
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         745
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         941
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         943
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ   SEQUENCE   1348 AA;  144279 MW;  2A4001CBE41D30D4 CRC64;
     MMVLEGASAL SPFRRARLET RLQTLVPALR LTGAWHVYFI RADAGRTPDQ ATLQRILQAE
     PAPAPRDEAA SSRYVVPRLG TLSPWSSKAT ELMRGAGQPI QRVERGTRID LAGWPEGEAD
     QAAVAKLLHD PMTQSLLGSA AAAEALFNVP DPGQLERIPL DALEQANGDL GLALAQDEID
     YLRERFAALG RDPADVELMM FAQANSEHCR HKIFNASWTI DGKPQERSLF RMIKHTHQQT
     PQHTLSAYSD NAAVVEGVPA ARFRPDPATG EYRSEAVVPS AFAIKVETHN HPTAIAPFPG
     AATGAGGEIR DEGATGRGGK PKAGLTGFSV SHLRIPTLPQ PWEAPRALNP RMAPALDIML
     DGPLGGAAFN NEFGRPNLLG YFRSFELAEG QGLTRAYDKP IMLAGGLGAI DRNQVEKLRL
     QPGDAVIVLG GPAMLIGLGG GAASSVAAGD SAEALDFASV QRENPEMERR CQEVIDHCVA
     LGTDNPIRWF HDVGAGGLSN AIPELLHDSG VGGVIDLARV PSDDPSLSPL ELWCNESQER
     YVLGVPQARL DEFAAICARE RCPFAAVGVA TAEERLVVGY GVFDAANRES GIGNRNSALP
     AAEAASAHSL FPTPDSPLPI NLPMDVLFGK APKMHRDAVH PAAPQWPVLQ TGALDLQEAG
     LRVLAHPTVA SKSFLVTIGD RSVGGLTARE QMIGPWQLPL ADCAITLAGF ETFDGEAMSI
     GERTPLALLN AAASARMAVG EAITNLCAAP VQTLDSIKLS ANWMAAAGHA GEDALLYDAV
     RAVGMELCPA LELSIPVGKD SLSMQAQWQV GNGESGIGNG ETPAPSASAI PDSRLPIPGE
     TLKSVSPVSL IISAFAPVSD VRTQLTPLLQ REDESELWLI GLGGGKQRLG GSVLAQVYAD
     DSALPAFGGE TPDLDDPQRL RQFFELIRDA REGGLLLAYH DRSDGGAFAA LCEMAFASRQ
     GLDITLDAWG DDAFRSLFNE ELGAVVQIAN EDRAAFADLV ERHALTECAQ RIARPTGTPR
     VRVSGQGRVL AEWRWEALFD AWWSVTHAMQ KLRDNPDSAD EERAVARNFQ APGLRPKLVF
     DPSEDVAAPF VATGARPKVA ILREQGVNGQ IEMAYNFERA GFRAFDVHMS DLIEGRVDLA
     QFAGFAACGG FSYGDVLGAG RGWATSILER AALRDAFAAF FARSDTFALG VCNGCQMLSQ
     LKDIIPGAEH WPRFLRNRSE QFEARTALLE VVESPSILLR GMAGSRIPVA VAHGEGRAEF
     DTAVDQAAAR VALRFIDGDG AVASQYPLNP NGSPDGITGL TSTDGRATIL MPHPERTPRS
     VNLSWHPAGW GEDSPWLRMF RNARVWCG
//