PUR4_XANCP
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 03-AUG-2022, entry version 125.
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=XCC0656;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; 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=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; AE008922; AAM39972.1; -; Genomic_DNA.
DR RefSeq; NP_636048.1; NC_003902.1.
DR RefSeq; WP_011035897.1; NC_003902.1.
DR AlphaFoldDB; Q8PCQ7; -.
DR SMR; Q8PCQ7; -.
DR STRING; 340.xcc-b100_3698; -.
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 OMA; LSANWMW; -.
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: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; 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
