ID   A0A3A1VUF4_STAAU        Unreviewed;       729 AA.
AC   A0A3A1VUF4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   31-JUL-2019, entry version 7.
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:GBV20637.1};
GN   ORFNames=M1K003_1631 {ECO:0000313|EMBL:GBV20637.1};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280 {ECO:0000313|EMBL:GBV20637.1, ECO:0000313|Proteomes:UP000265645};
RN   [1] {ECO:0000313|EMBL:GBV20637.1, ECO:0000313|Proteomes:UP000265645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1K003 {ECO:0000313|EMBL:GBV20637.1,
RC   ECO:0000313|Proteomes:UP000265645};
RA   Nakamura Y., Takahashi H., Takaya A., Inoue Y., Katayama Y.,
RA   Kusuya Y., Shoji T., Takada S., Nakagawa S., Oguma R., Ozawa N.,
RA   Yamaide F., Suzuki S., Villaruz A., Otto M., Matsue H., Nunez G.,
RA   Shimojo N.;
RT   "Protection against atopic dermatitis through acquisition of
RT   Staphylococcus quorum-sensing agr mutations in the skin.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC       complex involved in the purines biosynthetic pathway. Catalyzes
CC       the ATP-dependent conversion of formylglycinamide ribonucleotide
CC       (FGAR) and glutamine to yield formylglycinamidine ribonucleotide
CC       (FGAM) and glutamate. The FGAM synthase complex is composed of
CC       three subunits. PurQ produces an ammonia molecule by converting
CC       glutamine to glutamate. PurL transfers the ammonia molecule to
CC       FGAR to form FGAM in an ATP-dependent manner. PurS interacts with
CC       PurQ and PurL and is thought to assist in the transfer of the
CC       ammonia molecule from PurQ to PurL. {ECO:0000256|HAMAP-
CC       Rule:MF_00420}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-D-
CC         ribosyl)glycinamide = 2-(formamido)-N(1)-(5-phospho-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:58426, ChEBI:CHEBI:58478,
CC         ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00420, ECO:0000256|SAAS:SAAS01143401};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-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, ECO:0000256|SAAS:SAAS01143431}.
CC   -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1
CC       PurL, 1 PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-
CC       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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00420}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GBV20637.1}.
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DR   EMBL; BDVT01000007; GBV20637.1; -; Genomic_DNA.
DR   RefSeq; WP_000032740.1; NZ_UHCV01000002.1.
DR   KEGG; saud:CH52_00540; -.
DR   KO; K23269; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000265645; 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|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143413};
KW   Complete proteome {ECO:0000313|Proteomes:UP000265645};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143366};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143383};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143388};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143406};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143445}.
FT   REGION       99    102       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00420}.
FT   ACT_SITE     54     54       {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   ACT_SITE    100    100       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL        98     98       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       122    122       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       273    273       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       533    533       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING      57     57       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING      96     96       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     121    121       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     245    245       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     495    495       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     532    532       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     535    535       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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
//