ID   A0A3A1VUF4_STAAU        Unreviewed;       729 AA.
AC   A0A3A1VUF4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   05-FEB-2025, entry version 36.
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=DQU50_00960 {ECO:0000313|EMBL:TXL47676.1}, DQV00_13335
GN   {ECO:0000313|EMBL:TXL50599.1}, G0Z31_07080
GN   {ECO:0000313|EMBL:NGK21279.1}, G6Y24_06020
GN   {ECO:0000313|EMBL:NGW67053.1}, GQX52_12005
GN   {ECO:0000313|EMBL:NUY69343.1}, M1K003_1631
GN   {ECO:0000313|EMBL:GBV20637.1}, SAMEA70153168_01576
GN   {ECO:0000313|EMBL:CAC8237353.1};
OS   Staphylococcus aureus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280 {ECO:0000313|EMBL:NGW67053.1, ECO:0000313|Proteomes:UP000473113};
RN   [1] {ECO:0000313|Proteomes:UP000265645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1K003 {ECO:0000313|Proteomes:UP000265645};
RA   Nakamura Y., Takahashi H., Takaya A., Inoue Y., Katayama Y., Kusuya Y.,
RA   Shoji T., Takada S., Nakagawa S., Oguma R., Ozawa N., Yamaide F.,
RA   Suzuki S., Villaruz A., Otto M., Matsue H., Nunez G., Shimojo N.;
RT   "Protection against atopic dermatitis through acquisition of Staphylococcus
RT   quorum-sensing agr mutations in the skin.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000451682, ECO:0000313|Proteomes:UP000460821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt013 {ECO:0000313|EMBL:TXL47676.1}, pt013
RC   {ECO:0000313|Proteomes:UP000451682}, Pt061.1
RC   {ECO:0000313|EMBL:TXL50599.1}, and pt061.1
RC   {ECO:0000313|Proteomes:UP000460821};
RA   Sullivan M.J., Altman D.R., Chacko K., Ciferri B., Webster E., Deikus G.,
RA   Lewis M., Khan Z., Beckford C., Rendo A., Samaroo F., Sebra R.,
RA   Karam-Howlin R., Southwick K., Adams E., Ying L., Kornblum J., Factor S.,
RA   Danesh Yazdi M., Dingle T., Hamula C., Bashir A., Schadt E., Kasarskis A.,
RA   Patel G., Wallach F., Gibbs K., Van Bakel H.;
RT   "Whole genome sequencing to identify and define MRSA outbreaks.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:GBV20637.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M1K003 {ECO:0000313|EMBL:GBV20637.1};
RA   Nakamura Y., Takahashi H., Takaya A., Inoue Y., Katayama Y., Kusuya Y.,
RA   Shoji T., Takada S., Nakagawa S., Oguma R., Ozawa N., Yamaide F.,
RA   Suzuki S., Villaruz A., Otto M., Matsue H., Nunez G., Shimojo N.;
RT   "Protection against atopic dermatitis through acquisition of Staphylococcus
RT   quorum-sensing agr mutations in the skin.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:NUY69343.1, ECO:0000313|Proteomes:UP000561555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UP89 {ECO:0000313|EMBL:NUY69343.1,
RC   ECO:0000313|Proteomes:UP000561555};
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|EMBL:NGW67053.1, ECO:0000313|Proteomes:UP000473113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UG255 {ECO:0000313|EMBL:NGW67053.1,
RC   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:NGK21279.1, ECO:0000313|Proteomes:UP000478431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UP127 {ECO:0000313|EMBL:NGK21279.1,
RC   ECO:0000313|Proteomes:UP000478431};
RA   Carvajal L.P., Rincon S., Echeverri A., Porras J., Rios R., Ordonez K.,
RA   Seas C., Gomez-Villegas S., Diaz L., Arias C.A., Reyes J.;
RT   "Novel Insights Into The Classification of Staphylococcal Beta-Lactamases
RT   In Relation To The Cefazolin Inoculum Effect.";
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:CAC8237353.1, ECO:0000313|Proteomes:UP000507402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MOS114 {ECO:0000313|EMBL:CAC8237353.1,
RC   ECO:0000313|Proteomes:UP000507402};
RG   Pathogen Informatics;
RL   Submitted (JUN-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=N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + L-
CC         glutamine + ATP + H2O = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC         ribosyl)acetamidine + L-glutamate + ADP + phosphate + H(+);
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: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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NGW67053.1}.
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DR   EMBL; CAIIGN010000005; CAC8237353.1; -; Genomic_DNA.
DR   EMBL; BDVT01000007; GBV20637.1; -; Genomic_DNA.
DR   EMBL; JAAJIY010000017; NGK21279.1; -; Genomic_DNA.
DR   EMBL; JAALTR010000170; NGW67053.1; -; Genomic_DNA.
DR   EMBL; JAANDN010000108; NUY69343.1; -; Genomic_DNA.
DR   EMBL; QNXF01000001; TXL47676.1; -; Genomic_DNA.
DR   EMBL; QNXM01000003; TXL50599.1; -; Genomic_DNA.
DR   RefSeq; WP_000032740.1; NZ_WYCZ01000003.1.
DR   KEGG; saud:CH52_00540; -.
DR   OMA; AIHPTPV; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000265645; Unassembled WGS sequence.
DR   Proteomes; UP000451682; Unassembled WGS sequence.
DR   Proteomes; UP000460821; Unassembled WGS sequence.
DR   Proteomes; UP000473113; Unassembled WGS sequence.
DR   Proteomes; UP000478431; Unassembled WGS sequence.
DR   Proteomes; UP000507402; Unassembled WGS sequence.
DR   Proteomes; UP000561555; 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   CDD; cd02203; PurL_repeat1; 1.
DR   CDD; cd02204; PurL_repeat2; 1.
DR   FunFam; 3.30.1330.10:FF:000004; Phosphoribosylformylglycinamidine synthase subunit PurL; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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   NCBIfam; TIGR01736; FGAM_synth_II; 1.
DR   PANTHER; PTHR43555; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR   PANTHER; PTHR43555:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 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; SSF56042; PurM C-terminal domain-like; 2.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
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|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00420};
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}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00420}.
FT   DOMAIN          13..58
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          79..194
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          207..361
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          440..557
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
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   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         98
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         99..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         273
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         495
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         532
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         533
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT   BINDING         535
FT                   /ligand="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
//