PURL_BRASB
ID PURL_BRASB Reviewed; 735 AA.
AC A5EMI1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00420};
DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00420};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
DE Short=FGAR amidotransferase II {ECO:0000255|HAMAP-Rule:MF_00420};
DE Short=FGAR-AT II {ECO:0000255|HAMAP-Rule:MF_00420};
DE AltName: Full=Glutamine amidotransferase PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00420}; OrderedLocusNames=BBta_5401;
OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=288000;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTAi1 / ATCC BAA-1182;
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC complex involved in the purines biosynthetic pathway. Catalyzes the
CC ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and
CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and
CC glutamate. The FGAM synthase complex is composed of three subunits.
CC PurQ produces an ammonia molecule by converting glutamine to glutamate.
CC PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-
CC dependent manner. PurS interacts with PurQ and PurL and is thought to
CC assist in the transfer of the ammonia molecule from PurQ to PurL.
CC {ECO:0000255|HAMAP-Rule:MF_00420}.
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_00420};
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_00420}.
CC -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1 PurL,
CC 1 PurQ and 2 PurS subunits. {ECO:0000255|HAMAP-Rule:MF_00420}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}.
CC -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000255|HAMAP-
CC Rule:MF_00420}.
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DR EMBL; CP000494; ABQ37375.1; -; Genomic_DNA.
DR RefSeq; WP_012045339.1; NC_009485.1.
DR AlphaFoldDB; A5EMI1; -.
DR SMR; A5EMI1; -.
DR STRING; 288000.BBta_5401; -.
DR PRIDE; A5EMI1; -.
DR EnsemblBacteria; ABQ37375; ABQ37375; BBta_5401.
DR KEGG; bbt:BBta_5401; -.
DR eggNOG; COG0046; Bacteria.
DR HOGENOM; CLU_003100_0_1_5; -.
DR OMA; FIEPYQG; -.
DR OrthoDB; 26038at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000246; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion 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 Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.90.650.10; -; 2.
DR HAMAP; MF_00420; PurL_2; 1.
DR InterPro; IPR010074; PRibForGlyAmidine_synth_PurL.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR PANTHER; PTHR43555; PTHR43555; 1.
DR Pfam; PF00586; AIRS; 2.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR PIRSF; PIRSF001587; FGAM_synthase_II; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..735
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurL"
FT /id="PRO_1000050299"
FT ACT_SITE 48
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 93..96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 311..313
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 532
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
SQ SEQUENCE 735 AA; 78068 MW; 8AFFA6FB1CDD7BBC CRC64;
MRNEPQITPD LVAAHGLKPD EYERILKLIG RVPTFTELGI FSAMWNEHCS YKSSRIHLRG
LPTKAPWVIQ GPGENAGVID IGDGQAVVFK MESHNHPSYI EPYQGATTGV GGILRDVFTM
GARPIACLNA LSFGAPEHPK TRHLVSGVVA GIGGYGNSFG VPTVGGQTRF HTRYDGNILV
NAMAVGLADA DKIFYAAASG VNMPIVYLGS KTGRDGIHGA SMASAEFDDS SEEKRPTVQV
GDPFAEKLLL EACLEIMAAD CVIAIQDMGA AGLTCSAVEM GAKGDLGVDL DLDAVPTRET
GMSAYEMMLS ESQERMLMVL KPEKEKEAEA IFRKWGLDFA VVGYTTPSKR FVVKHGGDVM
ADLPIKELGD EAPLYDRPHV ASPALPVIHA REVKAPMDII PALEKLIATP DLCSKRWIWE
QYDHVILGNT VQRPGGDAAV VRVQDGPKGL ALTVDVTPRY CEADPYQGGM QAVAEAWRNI
TAVGGRPLAI TDNLNFGNPE RPEIMGQFVG CLKGISEACR ALDFPVVSGN VSLYNETNGR
AILPTPSIGG VGLLDDFTKS ASIAFEAEGE AILLIGETHG WLGQSVYLRD VCGREEGAPP
PVDLAAEKRI GDVVRGMIHA GTATAAHDLS DGGLLVALAE MAMASGIGAR LLAAPASIVP
HAYWFGEDQA RYLVTVPETE AGRVLAKMRG AGVPCTRIGT TGGSALAIAG EASVEVTTLK
TRFESWLPGY MGGAA
