ID A0A5E8F4G9_WEICO Unreviewed; 740 AA. AC A0A5E8F4G9; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 19-JAN-2022, entry version 9. 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:CCF30326.1}; GN ORFNames=WEISSC39_04175 {ECO:0000313|EMBL:CCF30326.1}; OS Weissella confusa LBAE C39-2. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Weissella. OX NCBI_TaxID=1127131 {ECO:0000313|EMBL:CCF30326.1, ECO:0000313|Proteomes:UP000004839}; RN [1] {ECO:0000313|EMBL:CCF30326.1, ECO:0000313|Proteomes:UP000004839} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LBAE C39-2 {ECO:0000313|EMBL:CCF30326.1, RC ECO:0000313|Proteomes:UP000004839}; RA Amari M., Laguerre S., Gabriel V., Moulis C., Loux V., Klopp C., Robert H., RA Gabriel B., Vuillemin M., Morel S., Remaud-Simeon M., Fontagne-Faucher C.; RT "Genome sequence of Weissella confusa LBAE C39-2 isolated from a wheat RT sourdough."; RL Submitted (DEC-2011) 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; CC Evidence={ECO:0000256|ARBA:ARBA00000910, 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 --------------------------------------------------------------------------- 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; CAGH01000007; CCF30326.1; -; Genomic_DNA. DR RefSeq; WP_003608196.1; NZ_CAGH01000007.1. DR STRING; 1127131.WEISSC39_04175; -. DR GeneID; 57978468; -. DR UniPathway; UPA00074; UER00128. DR Proteomes; UP000004839; 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; 2. 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00420}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00420}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, 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 17..61 FT /note="FGAR-AT_linker" FT /evidence="ECO:0000259|Pfam:PF18072" FT DOMAIN 95..197 FT /note="AIRS" FT /evidence="ECO:0000259|Pfam:PF00586" FT DOMAIN 210..364 FT /note="AIRS_C" FT /evidence="ECO:0000259|Pfam:PF02769" FT DOMAIN 447..563 FT /note="AIRS" FT /evidence="ECO:0000259|Pfam:PF00586" FT DOMAIN 578..709 FT /note="AIRS_C" FT /evidence="ECO:0000259|Pfam:PF02769" FT REGION 102..105 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT REGION 322..324 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT ACT_SITE 57 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT ACT_SITE 103 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT METAL 101 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT METAL 125 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT METAL 278 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT METAL 540 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 60 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 99 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 124 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 248 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 502 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 539 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" FT BINDING 542 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420" SQ SEQUENCE 740 AA; 78677 MW; 52E60D0B8349DBBC CRC64; MTTATTTYEP TAEMVRDEKM YLAWGLTEAE YDLIVAKLDR LPNYTEAGLF SAMWSEHVSY KKSKPVLRTF WSRNERVLQG PGEGAGILDI GDGQAVVFKA ESHNHPSAVE PYEGAATGVG GILRDIFSMG AQPIAVLDSL RFGELNNATT KHLLDGVIAG IAGYGNAIGI PTVGGEIGFD AVYQGNPLVN VMAVGVIDQA AMQVGRAEGV GNTVMYVGAK TGRDGIHGAT FASAEFSSDE DQNRSAVQVG DPFMEKLVMD ATLKAIREHG DVIVGVQDMG AAGLVSSSAE MAGKAGMGMQ LNLDLVPQRE TGMTPYELML SESQERMLLV VAAGHEAEVQ AVFEDAGLDA VAVGTVTDTG RYELLWHGDV AANVPVDFLT TAPKQEMPQA TPTRLNEPSA DFVPGTLDGA ATLTELLQQP TIASKASLFR HFDSMVRADT VVKPGGDAAV VRLRGTKKAL AMTTDVNSRF TYLDPYIGGQ LAVVEAAGNV VATGAQPIGI TDCLNFGNPD DPEIYYELAQ SVAGINQMAK QLNTPVISGN VSLYNETDGQ AIYPTPMVGM VGLHEDVKMI TTISFKNAGD VIYVLGETAA DFNGSELQKM VTGDVSGRLR GFDMTEIQTT QAKLLDAIAA DLVASAHDIA EGGLGVALAE STFKTPFGAT MQWQVPTAWL FSETPGRFVV SVPEANVAVF EQLMGDTATK LGVVTAGDTI QMNTEADELN LSKTTLQENY EEAITWQRNQ //