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PURL_MYCLB
ID   PURL_MYCLB              Reviewed;         754 AA.
AC   B8ZSV5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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}; OrderedLocusNames=MLBr02211;
OS   Mycobacterium leprae (strain Br4923).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=561304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Br4923;
RX   PubMed=19881526; DOI=10.1038/ng.477;
RA   Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA   Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA   Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA   Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA   Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA   Rougemont J., Brennan P.J., Cole S.T.;
RT   "Comparative genomic and phylogeographic analysis of Mycobacterium
RT   leprae.";
RL   Nat. Genet. 41:1282-1289(2009).
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; FM211192; CAR72308.1; -; Genomic_DNA.
DR   RefSeq; WP_010908771.1; NC_011896.1.
DR   AlphaFoldDB; B8ZSV5; -.
DR   SMR; B8ZSV5; -.
DR   EnsemblBacteria; CAR72308; CAR72308; MLBr02211.
DR   KEGG; mlb:MLBr02211; -.
DR   HOGENOM; CLU_003100_0_1_11; -.
DR   OMA; FIEPYQG; -.
DR   OrthoDB; 26038at2; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000006900; 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..754
FT                   /note="Phosphoribosylformylglycinamidine synthase subunit
FT                   PurL"
FT                   /id="PRO_1000206042"
FT   REGION          386..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   ACT_SITE        105
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         104..107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         280
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         324..326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         512
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         549
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         550
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         552
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
SQ   SEQUENCE   754 AA;  80131 MW;  AEC969914F0C9ECB CRC64;
     MIDTVEYAAT TPDQPQPFAE LGLREDEYQR VREILGRRPT DTELAMYSVM WSEHCSYKSS
     KVHLRYFGET TTEEMRTGML AGIGENAGVV DIGDGWAVTF KVESHNHPSY VEPYQGAATG
     VGGIVRDIMA MGARPVAVMD QLRFGAADAL DTRRVLDGVV RGIGGYGNSL GLPNIGGETV
     FDSCYDGNPL VNALCVGVLR QEDLHLAFAS GAGNKIILFG ACTGLDGIGG VSVLASDTFD
     AEGARKKLPS VQVGDPFMEK VLIECCLELY AGGLVIGIQD LGGAGLSCAT SELASAGDVG
     MAIQLDTVPR RAKDMTPAEV FCSESQERMC AVVAPENVDA FLAVCRKWEV LATVIGEVTD
     GDRLRITWHG ETVVDVPPRT VAHEGPVYQR PVSRPESQEA LNADSSKGLP RPVSGDELRA
     TLLALLGSPH LCSRAFITEQ YDRYVRGNTV LAEHADAGVL RIDESTGRGI ALSTDASGRY
     TRLDPYAGAQ LALAEAYRNV AVTGATPVAV TNCLNFGSPE DPGVMWQFAQ AVRGLADGCA
     ALKIPVTGGN VSFYNQTGAV AILPTPVVGV LGVLDNVARR IHTSLGTEPG EILMLLGDTY
     DEFDGSVWAQ VMAGHLGGLP PMVDLAREKL LAEVLSSASR DELVSAAHDL SEGGLAQAIV
     ESALAGETGC RIALPEDADP FVMLFSESAG RVLVAVPRPE ESRFRSMCEA RGLPAMRIGV
     VDQGSDSIEV RGQFTVSLAE LRMTFEAVLP RFFG
 
 
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