PUR4_XANAC
ID PUR4_XANAC Reviewed; 1348 AA.
AC Q8PGR7;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=XAC3549;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
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=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; AE008923; AAM38392.1; -; Genomic_DNA.
DR RefSeq; WP_011052353.1; NC_003919.1.
DR AlphaFoldDB; Q8PGR7; -.
DR SMR; Q8PGR7; -.
DR STRING; 190486.XAC3549; -.
DR EnsemblBacteria; AAM38392; AAM38392; XAC3549.
DR GeneID; 66912584; -.
DR KEGG; xac:XAC3549; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000576; 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..1348
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100424"
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; 144661 MW; 4F2ED1E821469A37 CRC64;
MMVLEGASAL SPFRRARLET RLQTLVPALR ITGAWHVYFI RPEAGQSPDQ ATLQRILQAN
AAPAERDADA SSRYVVPRLG TLSPWSSKAT ELVRGAGQPI QRVERGTRID LAGWPDDASA
QAAVAKLLHD PMTQSLLGSA AAAEALFNVP DPGQLRRVPL DGLEQANRDL GLALAQDEID
YLRERFGALG RDPADVELMM FAQANSEHCR HKIFNATWTI DGKPQERSLF RMIKHTHQQT
PQHTLSAYSD NAAVVEGVPA ARYRPDPATG QYRSEAVLPS AFAIKVETHN HPTAIAPFPG
AATGAGGEIR DEGATGRGGK PKAGLTGFSV SHLRIPTLPQ PWEAPRALNP RMAPALDIML
DGPLGGAAFN NEFGRPNLLG YFRSFELAEG PGLTRAYDKP IMLAGGLGAI DRNQVEKLRL
QPGDAVIVLG GPAMLIGLGG GAASSVAAGD SAEALDFASV QRENPEMERR CQEVIDRCVA
LGVDNPIRWF HDVGAGGLSN AIPELLHDSG VGGIIDLGRV LTDDPSLSPL ELWCNESQER
YVLGVPQARL EEFAAICARE RCPFAAVGVA TAEERLVVGY GVLDAGNRES GVGNRNGTLV
AADTASHHSP FPTRDSQLPI DLPMDVLFGK APKMHRDAAH PGAPQWPVLQ TASLDLQQAG
LRVLAHPTVA SKSFLVTIGD RSVGGLTARE QMIGPWQLPL ADCAITLAGF DTFEGEAMSI
GERTPLALLN AAASARMAVG EAITNLCAAP VQTLDSIKLS ANWMAAAGHS GEDALLYDAV
RAIGMELCPA LELSVPVGKD SLSMQAQWQV GNRESGIGNG ETPQPSASTI PDSPFPIPGE
TLKSVSPVSL IISAFAPVGD VRTQLTPLLR SGEESELWLI GLGGGKQRLG GSVLAQVYAD
DTALPAFGGE VPDLDDAQRL RSFFELIRDA RDSGLLLAYH DRSDGGAFAA LCEMAFASRQ
GLDITLDAWG DDAFRSLFNE ELGAVVQIAS EDRAAFADLV ERHALTECAQ RIARPTGTPR
IRVSGQGRVL AEWRWEELFD AWWSVTHAMQ KLRDNPDSAD EERALARDFK ASGLRPKLVF
DPSDDVAAPF VATGTRPKVA ILREQGVNGQ IEMAYNFERA GFRPYDVHMS DLIEGRVDLS
AFVGFAACGG FSYGDVLGAG RGWATSILER SALRDAFAAF FARSDTFALG VCNGCQMLSQ
LKDIIPGAEH WPRFLRNRSE QFEARTALLE VVESPSIFLR GMAGSRIPVA VAHGEGRAEF
DSAVDQAAAR VALRYIDGDG AVASQYPLNP NGSPDGITGL TSSDGRVTIL MPHPERTPRS
ANLSWYPVDW GDDSPWLRMF RNARVWCG
