ID A0AA91Z3F0_WOLPI Unreviewed; 1019 AA. AC A0AA91Z3F0; DT 27-MAR-2024, integrated into UniProtKB/TrEMBL. DT 27-MAR-2024, sequence version 1. DT 24-JUL-2024, entry version 3. 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 ORFNames=BTO27_03140 {ECO:0000313|EMBL:PBQ27664.1}; OS Wolbachia pipientis wAus. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=2049495 {ECO:0000313|EMBL:PBQ27664.1, ECO:0000313|Proteomes:UP000218032}; RN [1] {ECO:0000313|EMBL:PBQ27664.1, ECO:0000313|Proteomes:UP000218032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=wAus {ECO:0000313|Proteomes:UP000218032}; RA Ward C.M., Baxter S.W.; RT "Wolbachia endosymbiont of Plutella Australiana."; RL Submitted (DEC-2016) 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=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D- CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-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: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:PBQ27664.1}. 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; MRWX01000023; PBQ27664.1; -; Genomic_DNA. DR RefSeq; WP_007302652.1; NZ_MRWX01000023.1. DR Proteomes; UP000218032; 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 Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 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 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; 2. DR Pfam; PF18072; FGAR-AT_linker; 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|HAMAP-Rule:MF_00420}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00420}; KW Ligase {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 218..259 FT /note="Phosphoribosylformylglycinamidine synthase linker" FT /evidence="ECO:0000259|Pfam:PF18072" FT DOMAIN 296..425 FT /note="PurM-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00586" FT DOMAIN 441..589 FT /note="PurM-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF02769" FT DOMAIN 733..810 FT /note="PurM-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00586" FT DOMAIN 855..1001 FT /note="PurM-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF02769" FT ACT_SITE 256 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT ACT_SITE 316 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 312 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 314 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 337 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 338 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 477 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 505 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 546..548 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 770 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 807 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 810 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" SQ SEQUENCE 1019 AA; 112914 MW; A55368871BC21BE3 CRC64; MANIRIEVFN KCEQVSRRRV VNVYLIYISK ELPSKLHEEI CGLFYNKAIQ DCRYYSYNEN LEEVQYNFIE SQAKWGLEIS FLPGMTDNVG NTAKQIVREY LMSKRHIDES VSIKARSSKL ILSQGGFPTE DDIKQEFNPI TEYCTLFHKE NGNCHWKYYS KQNTPVGVIT ARDQEKKEWI PVSSTGMTPG NNGAKSVKLN VSDQELEKIS RDGIDGNGTL GLSLAAMKAI KDYFKKLGRN PYDIELESLA QTWSEHCKHN IFCSPIDEIK DGLYAHYIKR ATREINSNIC VSVFSDNAGG IIFDDDYLIV DKVETHNSPS ALDPFGGAMT GVLGVNRDIV GFGKGAEPIM NTYYFCFAKE SKGKLYRDKE RTDKILPPKY IMKEVIHGVN VAGNCSGIPT QLGSVYFDDR FCGKPLVFVG SIGIIPRNIN NAPSHIKEPK NGDKIVIIGG RVGRDGIHGA TFSSEALSGN SPSTIVQIGD PITQKKLSNA VVKARDLGLY NAITDNGAGG LSSSIGEMGK DGFEVDLSKV LLKNDGMAPW EIWISESQER MTLAVPEENL PAFKQIMKTH DVEVCVIGEF NKSGKAVVKC PPGEVIMDIE TEFLHDGNPK VHLQTKPWSK ESAVSFPVIP VLDTGIQQVK PANILRQNPY DGRAEREMDS SLSYLHDTFE LKEMLSRPNI RSKEFIVVQY DHEVQGSSIL KPLQGKGRVC SEAVVSRPVL SSNKGVVKSQ GFGSSYGEID TYHMAACAID TAIRNYVAAG GNINHLALLD NFCWCDAYNP ERLWQLKRAA EACYDFATAF KTPFISGKDS MFNDFKGYDE NGEKVMISAP PSLLISAIGI IDNIENAVSL DVKMPGDLIY VLGTTYDELG RSEYQLYSGI DNNNVPKVNA KSARKLYERY NQAIKDGIIV SAIAPNLGGL IIALAKSLIA GDLGAEIDLS LVPIGKTQNT DIINKIIMFS ESQSRILVTI APQNQRKFEE LFKGIVFSCI GKVTEEKALN IKDIIRIDLK DLGTSLNNF //