ID   A0A3A1VUF4_STAAU        Unreviewed;       729 AA.
AC   A0A3A1VUF4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   02-JUN-2021, entry version 20.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE            Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00420};
DE            EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00420};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
DE            Short=FGAR amidotransferase II {ECO:0000256|HAMAP-Rule:MF_00420};
DE            Short=FGAR-AT II {ECO:0000256|HAMAP-Rule:MF_00420};
DE   AltName: Full=Glutamine amidotransferase PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
GN   Name=purL {ECO:0000256|HAMAP-Rule:MF_00420,
GN   ECO:0000313|EMBL:NGW67053.1};
GN   ORFNames=BSG38_05780 {ECO:0000313|EMBL:APZ37002.1}, FPP48_05430
GN   {ECO:0000313|EMBL:QNW10157.1}, G6X35_11490
GN   {ECO:0000313|EMBL:NGV92008.1}, G6Y24_06020
GN   {ECO:0000313|EMBL:NGW67053.1}, GO706_02825
GN   {ECO:0000313|EMBL:MVI37619.1}, GQX47_05070
GN   {ECO:0000313|EMBL:NUW99178.1};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280 {ECO:0000313|EMBL:NGW67053.1, ECO:0000313|Proteomes:UP000473113};
RN   [1] {ECO:0000313|Proteomes:UP000187080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCI62 {ECO:0000313|Proteomes:UP000187080};
RA   Nicholson T.L., Bayles D.O., Hau S.J.;
RT   "Staphylococcus aureus UCI 62 MRSA ST5.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:APZ37002.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCI62 {ECO:0000313|EMBL:APZ37002.1};
RA   Nicholson T.L., Bayles D.O., Hau S.J.;
RT   "Staphylococcus aureus UCI62 MRSA ST5.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MVI37619.1, ECO:0000313|Proteomes:UP000433276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S_4044.LJLM.AI {ECO:0000313|EMBL:MVI37619.1,
RC   ECO:0000313|Proteomes:UP000433276};
RA   Stine O.C.;
RT   "Implementation of targeted gown and glove precautions to prevent
RT   Staphylococcus aureus acquisition in community-based nursing homes.";
RL   Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:NUW99178.1, ECO:0000313|Proteomes:UP000550415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UP686 {ECO:0000313|EMBL:NUW99178.1,
RC   ECO:0000313|Proteomes:UP000550415};
RX   PubMed=32562543;
RA   Castro B.E., Berrio M., Vargas M.L., Carvajal L.P., Millan L.V., Rios R.,
RA   Hernandez A.K., Rincon S., Cubides P., Forero E., Dinh A., Seas C.,
RA   Munita J.M., Arias C.A., Reyes J., Diaz L.;
RT   "Detection of heterogeneous vancomycin intermediate resistance in MRSA
RT   isolates from Latin America.";
RL   J. Antimicrob. Chemother. 0:0-0(2020).
RN   [5] {ECO:0000313|Proteomes:UP000473113, ECO:0000313|Proteomes:UP000474795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UB561 {ECO:0000313|EMBL:NGV92008.1,
RC   ECO:0000313|Proteomes:UP000474795}, and UG255
RC   {ECO:0000313|EMBL:NGW67053.1, ECO:0000313|Proteomes:UP000473113};
RA   Castro-Cardozo B., Berrio M., Vargas M.L., Carvajal L.P., Millan L.V.,
RA   Rios R., Hernandez A., Rincon S.L., Cubides P., Forero E., Dinh A.,
RA   Seas C., Munita J.M., Arias C.A., Reyes J., Diaz L.;
RT   "Detection of Heterogeneous Vancomycin Intermediate Resistance in
RT   Methicillin Resistant Staphylococcus aureus Isolates from Latin-America.";
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:QNW10157.1, ECO:0000313|Proteomes:UP000516842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt285 {ECO:0000313|EMBL:QNW10157.1}, and pt285
RC   {ECO:0000313|Proteomes:UP000516842};
RA   Caban A.B., Pak T., Kumaresh A., Dupper A., Chacko K., Sullivan M.J.,
RA   Altman D.R., van Bakel H.;
RT   "PathoSPOT genomic surveillance reveals prolonged under the radar outbreaks
RT   of nosocomial methicillin resistant S. aureus bloodstream infections.";
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000910, ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00420}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420}.
CC   -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00420}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00420}.
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DR   EMBL; CP018766; APZ37002.1; -; Genomic_DNA.
DR   EMBL; WPRC01000090; MVI37619.1; -; Genomic_DNA.
DR   EMBL; JAALTV010000397; NGV92008.1; -; Genomic_DNA.
DR   EMBL; JAALTR010000170; NGW67053.1; -; Genomic_DNA.
DR   EMBL; JAANDS010000007; NUW99178.1; -; Genomic_DNA.
DR   EMBL; CP049394; QNW10157.1; -; Genomic_DNA.
DR   RefSeq; WP_000032740.1; NZ_WYDB01000003.1.
DR   EnsemblBacteria; GBV20637; GBV20637; M1K003_1631.
DR   KEGG; saud:CH52_00540; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000187080; Chromosome.
DR   Proteomes; UP000433276; Unassembled WGS sequence.
DR   Proteomes; UP000473113; Unassembled WGS sequence.
DR   Proteomes; UP000474795; Unassembled WGS sequence.
DR   Proteomes; UP000516842; Chromosome.
DR   Proteomes; UP000550415; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00420};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00420};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00420, ECO:0000313|EMBL:NGW67053.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00420};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00420};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00420};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00420}.
FT   DOMAIN          14..58
FT                   /note="FGAR-AT_linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          89..194
FT                   /note="AIRS"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          207..360
FT                   /note="AIRS_C"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          452..557
FT                   /note="AIRS"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   REGION          99..102
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   ACT_SITE        100
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   METAL           98
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   METAL           122
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   METAL           273
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   METAL           533
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         57
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         96
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         121
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         245
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         495
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         532
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         535
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
SQ   SEQUENCE   729 AA;  79563 MW;  B9C034B3161966FC CRC64;
     MSKFIEPSVE EIKLEKVYQD MGLSDQEYEK VCDILGRQPN FTETGIFSVM WSEHCSYKHS
     KPFLKQFPTS GEHVLMGPGE GAGVVDIGDN QAVVFKVESH NHPSAIEPYQ GAATGVGGII
     RDIVSIGARP INLLNSLRFG ELDNKQNQRL LKGVVKGIGG YGNCIGIPTT AGEIEFDERY
     DGNPLVNAMC VGVINHDMIQ KGTAKGVGNS VIYVGLKTGR DGIHGATFAS EELTEESESK
     RPSVQIGDPF VGKKLMEATL EAITFDELVG IQDMGAAGLT SSSSEMAAKG GSGLHLRLEQ
     VPTREPGISP YEMMLSETQE RMLLVVEKGN EQKFLDLFDK HELDSAVIGE VTDTNRFVLT
     YDDEVYADIP VEPLADEAPV YILEGEEKDY NTSKNDYTHI DVKDTFFKLL KHPTIASKHY
     LYDQYDQQVG ANTIIKPGLQ ASVVRVEGTN KAIASTIDGE ARYVYNNPYE GGKMVVAEAY
     RNLIAVGATP LAMTDCLNYG SPEKKEIYQQ LIDSTKGMAE ACDILKTPVV SGNVSLYNET
     KGTSIFPTPV VGMVGLIENV NYLNDFEPQV GDKLYLIGDT KDDFGGSQLE KLIYGKVNHE
     FESLDLSSEV EKGESIKTAI REGLLSHVQT VGKGGLLITL AKLSAHYGLG LKSSIDITNA
     QLFSETQGRY VVSVKSGKTL NIDNAIEIGL LTDSDNFKVT TPYTEISENV SDIKQIWEGA
     IAQCLTTQD
//