ID   A0A3A1VUF4_STAAU        Unreviewed;       729 AA.
AC   A0A3A1VUF4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   16-JAN-2019, entry version 2.
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:RIX72406.1};
GN   ORFNames=CFZ97_06325 {ECO:0000313|EMBL:RJE33098.1}, CFZ98_07460
GN   {ECO:0000313|EMBL:RJE32248.1}, CFZ99_14925
GN   {ECO:0000313|EMBL:RJE28419.1}, D3232_07895
GN   {ECO:0000313|EMBL:RIX72406.1}, D3237_10970
GN   {ECO:0000313|EMBL:RIX53246.1}, D5R87_01865
GN   {ECO:0000313|EMBL:RJT62874.1}, D5R88_04850
GN   {ECO:0000313|EMBL:RJT71931.1}, M1C031_1386
GN   {ECO:0000313|EMBL:GBU56272.1}, M1C066_0779
GN   {ECO:0000313|EMBL:GBV07008.1}, M1K003_1631
GN   {ECO:0000313|EMBL:GBV20637.1}, M1K028_1959
GN   {ECO:0000313|EMBL:GBV51861.1}, M1K094_2143
GN   {ECO:0000313|EMBL:GBV92723.1}, M1K100_2522
GN   {ECO:0000313|EMBL:GBW03457.1}, M6C003_1778
GN   {ECO:0000313|EMBL:GBX01908.1}, M6C029_2561
GN   {ECO:0000313|EMBL:GBX20530.1}, M6C066_0202
GN   {ECO:0000313|EMBL:GBX71810.1}, M6C068_2280
GN   {ECO:0000313|EMBL:GBX76448.1}, M6K030_2428
GN   {ECO:0000313|EMBL:GBY09790.1}, M6K049_0099
GN   {ECO:0000313|EMBL:GBY33092.1}, M6K089_0936
GN   {ECO:0000313|EMBL:GBY80111.1}, M6K094_2058
GN   {ECO:0000313|EMBL:GBY83612.1}, M6K100_2313
GN   {ECO:0000313|EMBL:GBY91521.1}, M6K136_1870
GN   {ECO:0000313|EMBL:GBZ29630.1}, M6K137_1086
GN   {ECO:0000313|EMBL:GBZ31304.1}, M6K146_2106
GN   {ECO:0000313|EMBL:GBZ45153.1}, M6K198_1911
GN   {ECO:0000313|EMBL:GCA03256.1}, M6K224_1191
GN   {ECO:0000313|EMBL:GCA30803.1}, MA46_03575
GN   {ECO:0000313|EMBL:RIZ63915.1};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280 {ECO:0000313|EMBL:RIX72406.1};
RN   [1] {ECO:0000313|EMBL:RIZ63915.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SA33 {ECO:0000313|EMBL:RIZ63915.1};
RA   Van Tyne D., Dabul N., Camargo I., Gilmore M.S.;
RT   "Comparative genomics of S. aureus and E. faecalis strains from
RT   Brazil.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RJE28419.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E987 {ECO:0000313|EMBL:RJE33098.1}, P1108
RC   {ECO:0000313|EMBL:RJE32248.1}, and P1209
RC   {ECO:0000313|EMBL:RJE28419.1};
RA   Berrio M., Diaz L., Reyes J., Ardila J., Porras P., Carvajal L.P.,
RA   Rincon S., Rios R., Munita J.M., Arias C.A.;
RT   "Can Whole Genome Sequencing Identify Heterogeneous Vancomycin-
RT   Intermediate Staphylococcus aureus (hVISA) Isolates?";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:GBU56272.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M1C031 {ECO:0000313|EMBL:GBU56272.1}, M1C066
RC   {ECO:0000313|EMBL:GBV07008.1}, M1K003 {ECO:0000313|EMBL:GBV20637.1},
RC   M1K028 {ECO:0000313|EMBL:GBV51861.1}, M1K094
RC   {ECO:0000313|EMBL:GBV92723.1}, M1K100 {ECO:0000313|EMBL:GBW03457.1},
RC   M6C003 {ECO:0000313|EMBL:GBX01908.1}, M6C029
RC   {ECO:0000313|EMBL:GBX20530.1}, M6C066 {ECO:0000313|EMBL:GBX71810.1},
RC   M6C068 {ECO:0000313|EMBL:GBX76448.1}, M6K030
RC   {ECO:0000313|EMBL:GBY09790.1}, M6K049 {ECO:0000313|EMBL:GBY33092.1},
RC   M6K089 {ECO:0000313|EMBL:GBY80111.1}, M6K094
RC   {ECO:0000313|EMBL:GBY83612.1}, M6K100 {ECO:0000313|EMBL:GBY91521.1},
RC   M6K136 {ECO:0000313|EMBL:GBZ29630.1}, M6K137
RC   {ECO:0000313|EMBL:GBZ31304.1}, M6K146 {ECO:0000313|EMBL:GBZ45153.1},
RC   M6K198 {ECO:0000313|EMBL:GCA03256.1}, and M6K224
RC   {ECO:0000313|EMBL:GCA30803.1};
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.
RN   [4] {ECO:0000313|EMBL:RIX72406.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SAV1149 {ECO:0000313|EMBL:RIX72406.1}, and SAV1228
RC   {ECO:0000313|EMBL:RIX53246.1};
RA   Tegegne H.A., Boland C., Wattiau P., Florianova M., Gelbicova T.,
RA   Kolackova I., Karpiskova R.;
RT   "Genome Sequence of Livestock-Associated Methicillin Resistant
RT   Staphylococcus aureus Spa Type t899 belongs to the Three Different
RT   Sequence Types ST398, ST9 and ST4034 Isolates from the Czech
RT   Republic.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:RJT62874.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SABHZ053 {ECO:0000313|EMBL:RJT62874.1};
RA   Tang B., Zhang L., Chang J., Luo Y.;
RT   "Genome sequencing of Staphylococcus aureus strain SABHZ053.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:RJT71931.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SABHZ079 {ECO:0000313|EMBL:RJT71931.1};
RA   Tang B., Zhang L., Chang J., Luo Y.;
RT   "Genome sequencing of Staphylococcus aureus strain SABHZ079.";
RL   Submitted (SEP-2018) 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};
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}.
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:RIX72406.1}.
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DR   EMBL; BDUU01000004; GBU56272.1; -; Genomic_DNA.
DR   EMBL; BDVO01000001; GBV07008.1; -; Genomic_DNA.
DR   EMBL; BDVT01000007; GBV20637.1; -; Genomic_DNA.
DR   EMBL; BDWF01000004; GBV51861.1; -; Genomic_DNA.
DR   EMBL; BDWV01000005; GBV92723.1; -; Genomic_DNA.
DR   EMBL; BDWZ01000009; GBW03457.1; -; Genomic_DNA.
DR   EMBL; BDYN01000014; GBX01908.1; -; Genomic_DNA.
DR   EMBL; BDYU01000014; GBX20530.1; -; Genomic_DNA.
DR   EMBL; BDZP01000001; GBX71810.1; -; Genomic_DNA.
DR   EMBL; BDZQ01000013; GBX76448.1; -; Genomic_DNA.
DR   EMBL; BEAD01000011; GBY09790.1; -; Genomic_DNA.
DR   EMBL; BEAN01000001; GBY33092.1; -; Genomic_DNA.
DR   EMBL; BEBF01000004; GBY80111.1; -; Genomic_DNA.
DR   EMBL; BEBG01000007; GBY83612.1; -; Genomic_DNA.
DR   EMBL; BEBJ01000013; GBY91521.1; -; Genomic_DNA.
DR   EMBL; BEBY01000008; GBZ29630.1; -; Genomic_DNA.
DR   EMBL; BEBZ01000004; GBZ31304.1; -; Genomic_DNA.
DR   EMBL; BECE01000006; GBZ45153.1; -; Genomic_DNA.
DR   EMBL; BEDB01000015; GCA03256.1; -; Genomic_DNA.
DR   EMBL; BEDM01000005; GCA30803.1; -; Genomic_DNA.
DR   EMBL; QYAQ01000025; RIX53246.1; -; Genomic_DNA.
DR   EMBL; QYAT01000047; RIX72406.1; -; Genomic_DNA.
DR   EMBL; JROJ01000002; RIZ63915.1; -; Genomic_DNA.
DR   EMBL; NMOP01000145; RJE28419.1; -; Genomic_DNA.
DR   EMBL; NMOQ01000061; RJE32248.1; -; Genomic_DNA.
DR   EMBL; NMOR01000049; RJE33098.1; -; Genomic_DNA.
DR   EMBL; QZVV01000003; RJT62874.1; -; Genomic_DNA.
DR   EMBL; QZVW01000006; RJT71931.1; -; Genomic_DNA.
DR   RefSeq; WP_000032740.1; NZ_UHCV01000002.1.
DR   UniPathway; UPA00074; UER00128.
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; 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   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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00420, ECO:0000313|EMBL:RIX72406.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   DOMAIN       89    194       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      207    360       AIRS_C. {ECO:0000259|Pfam:PF02769}.
FT   DOMAIN      452    557       AIRS. {ECO:0000259|Pfam:PF00586}.
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
//