PURL_STAS1
ID PURL_STAS1 Reviewed; 729 AA.
AC Q49WJ3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=SSP1721;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18866.1; -; Genomic_DNA.
DR RefSeq; WP_011303436.1; NZ_MTGA01000039.1.
DR AlphaFoldDB; Q49WJ3; -.
DR SMR; Q49WJ3; -.
DR STRING; 342451.SSP1721; -.
DR EnsemblBacteria; BAE18866; BAE18866; SSP1721.
DR KEGG; ssp:SSP1721; -.
DR PATRIC; fig|342451.11.peg.1720; -.
DR eggNOG; COG0046; Bacteria.
DR HOGENOM; CLU_003100_0_1_9; -.
DR OMA; FIEPYQG; -.
DR OrthoDB; 26038at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000006371; 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; 1.
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; Reference proteome.
FT CHAIN 1..729
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurL"
FT /id="PRO_0000236668"
FT ACT_SITE 54
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT ACT_SITE 100
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 99..102
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 317..319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 535
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
SQ SEQUENCE 729 AA; 79461 MW; F17DF35C9B1B82E0 CRC64;
MSKFIEPSSE DIKIEQLYKD MGLSDEEYAK VCDILGREPN FTEIGIFSVM WSEHCSYKHS
KPFLTQFPTS GEHVLMGPGE GAGVVDIGDN QAVVFKVESH NHPSAVEPYQ GAATGVGGII
RDIVSIGARP INLLNSLRFG ELTEKQNRRL LRGVVAGIGG YGNCIGIPTT AGEIEFDDRY
DGNPLVNAMC VGIIDHDMVQ KGTAKGVGNS VIYVGLKTGR DGIHGATFAS EELSEDSESK
RPSVQIGDPF VGKKLMEATL EAITFDELVG IQDMGAAGLT SSSSEMAAKG GSGLHLRLEQ
VPTREQGISP YEMMLSETQE RMLLVVEKGT EQKFLDLFDK HELDSAVIGE VTDTDRFVLT
YEDEVFADIP VQPLSDEAPV YVLEGTSPEY NETKNDYSSV DVESVFDQLL QHPTIASKRY
LYEQYDQQVG ANTIVKPGLQ ASVVRVEGTD KAIASTIDGE ARYVFNNPYE GGKIVVAEAY
RNLISVGATP LAMTDCLNYG SPEKKEIYQQ LADSTKGMAE ACEVLSTPVV SGNVSLYNET
RETSIFPTPV VGMVGLIDDI SYLNHFNPSV GDTLYVVGDT NDDFGGSQIE KLLYGQVNHE
FESIDLSQEV RKGESIKQAI REGVASHVQT VGKGGLLLTL ARISAHYQLG LQAKLSVTNA
QLFSETQGRY IVIVKNGQSL NCDYAVEIGK VTNDQQFKVT NEQSEIVRDV KHLNDLWEGA
IPQCMTATD
