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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //