ID   A0A3A1VUF4_STAAU        Unreviewed;       729 AA.
AC   A0A3A1VUF4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   26-FEB-2020, entry version 12.
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}, SAKG03_09690
GN   {ECO:0000313|EMBL:BBJ12331.1};
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., 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|EMBL:BBJ12331.1, ECO:0000313|Proteomes:UP000326733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KG-03 {ECO:0000313|EMBL:BBJ12331.1,
RC   ECO:0000313|Proteomes:UP000326733};
RX   PubMed=31474962;
RA   Kuroda M., Sekizuka T., Matsui H., Ohsuga J., Ohshima T., Hanaki H.;
RT   "IS256-Mediated Overexpression of the WalKR Two-Component System Regulon
RT   Contributes to Reduced Vancomycin Susceptibility in a Staphylococcus aureus
RT   Clinical Isolate.";
RL   Front. Microbiol. 10:1882-1882(2019).
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-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; 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, ECO:0000256|SAAS:SAAS01143431}.
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; AP019542; BBJ12331.1; -; Genomic_DNA.
DR   EMBL; BDVT01000007; GBV20637.1; -; Genomic_DNA.
DR   RefSeq; WP_000032740.1; NZ_WBHU01000005.1.
DR   SMR; A0A3A1VUF4; -.
DR   KEGG; saud:CH52_00540; -.
DR   KO; K23269; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000265645; Unassembled WGS sequence.
DR   Proteomes; UP000326733; 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 {ECO:0000256|HAMAP-Rule:MF_00420,
KW   ECO:0000256|SAAS:SAAS01143413};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00420, ECO:0000256|SAAS:SAAS01143366};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00420, 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   DOMAIN          15..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
//