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PURL_CAMJJ
ID   PURL_CAMJJ              Reviewed;         728 AA.
AC   A1VZU6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE            Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00420};
DE            EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00420};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
DE            Short=FGAR amidotransferase II {ECO:0000255|HAMAP-Rule:MF_00420};
DE            Short=FGAR-AT II {ECO:0000255|HAMAP-Rule:MF_00420};
DE   AltName: Full=Glutamine amidotransferase PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
GN   Name=purL {ECO:0000255|HAMAP-Rule:MF_00420};
GN   OrderedLocusNames=CJJ81176_0978;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) 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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00420}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}.
CC   -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00420}.
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DR   EMBL; CP000538; EAQ71846.1; -; Genomic_DNA.
DR   RefSeq; WP_002853351.1; NC_008787.1.
DR   AlphaFoldDB; A1VZU6; -.
DR   SMR; A1VZU6; -.
DR   STRING; 354242.CJJ81176_0978; -.
DR   EnsemblBacteria; EAQ71846; EAQ71846; CJJ81176_0978.
DR   KEGG; cjj:CJJ81176_0978; -.
DR   eggNOG; COG0046; Bacteria.
DR   HOGENOM; CLU_003100_0_1_7; -.
DR   OMA; FIEPYQG; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000000646; 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; 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; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..728
FT                   /note="Phosphoribosylformylglycinamidine synthase subunit
FT                   PurL"
FT                   /id="PRO_1000050305"
FT   ACT_SITE        42
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   ACT_SITE        88
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         87..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         110
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         309..311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         491
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         528
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         529
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         531
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
SQ   SEQUENCE   728 AA;  79320 MW;  A735E7432F7DF78A CRC64;
     MDKETIKAHK ISDEEYAQIL EILGREPNLL ELGVISAMWS EHCSYKSSKK YLNGFPTKAP
     WVIQGPGENA GVIDIGQGMA AVFKVESHNH PSFIEPFAGA ATGVGGILRD VFTMGARVVA
     GLNSLKFGDI HDEKCGKHQK YLVKGVVNGI SHYGNCMGVP TIGGECAFDE CFNGNILVNA
     FALGVCKSED IFYAKAEGVG NPVIYVGSKT GRDGLGGAVM ASDSFNEESK SLRPTVQIGD
     PFSEKLLMEA CLELFKTDYI VGIQDMGAAG LTSSSFEMAG RSGSGMKLYL DKTPMRESGM
     TPYELMLSES QERMLICAKK GYEDKVIEIF KKWDLDAVVM GEVTNTGKME LFWHDELVGL
     IPIEPLSEKA PILSRPTSEP KYLSEIKNYK FELKSSVQEL FIQMLQNENI NNKAFIYDQF
     DSSVQTNTIK ADGRLGASVI RIKENGASVA MAIECNSRLN YVNPKIGAAL AVASAGRKVA
     CTGAKPLAIS DCLNYGNPQN PEVMWQFAQG CEGIKEACKE LNTPVVSGNV SLYNETEGVS
     IYPSPTIVSV GVLEDANKTL KASFEKENLS VYLLGESLGE FSGSMVMKIQ DKKVSGSLKE
     LDYKAELALW DLLYKANQNS LLECANSVGI GGIAMTLAKM FAISSVGANL TSDFDDEKMI
     FDESASRAII GLSKENEEAF LNLAKEFGVK AYKLGVSTSQ KHFKLDSIEL SKAELDKLYF
     ESFKEQIQ
 
 
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