PURL_MYCTO
ID PURL_MYCTO Reviewed; 766 AA.
AC P9WHL6; L0T4Y4; O06631; P0A5T8; P54876;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 2.
DT 03-AUG-2022, entry version 40.
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=MT0823;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK45065.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000250|UniProtKB:P9WHL7};
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DR EMBL; AE000516; AAK45065.1; ALT_INIT; Genomic_DNA.
DR PIR; D70536; D70536.
DR AlphaFoldDB; P9WHL6; -.
DR SMR; P9WHL6; -.
DR EnsemblBacteria; AAK45065; AAK45065; MT0823.
DR KEGG; mtc:MT0823; -.
DR HOGENOM; CLU_003100_0_1_11; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001020; 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..766
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurL"
FT /id="PRO_0000428163"
FT ACT_SITE 66
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT ACT_SITE 117
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 116..119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 336..338
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 561
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 562
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 564
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
SQ SEQUENCE 766 AA; 80801 MW; 31943EABED74021E CRC64;
MSPLARTPRK TSVLDTVEHA ATTPDQPQPY GELGLKDDEY RRIRQILGRR PTDTELAMYS
VMWSEHCSYK SSKVHLRYFG ETTSDEMRAA MLAGIGENAG VVDIGDGWAV TFKVESHNHP
SYVEPYQGAA TGVGGIVRDI MAMGARPVAV MDQLRFGAAD APDTRRVLDG VVRGIGGYGN
SLGLPNIGGE TVFDPCYAGN PLVNALCVGV LRQEDLHLAF ASGAGNKIIL FGARTGLDGI
GGVSVLASDT FDAEGSRKKL PSVQVGDPFM EKVLIECCLE LYAGGLVIGI QDLGGAGLSC
ATSELASAGD GGMTIQLDSV PLRAKEMTPA EVLCSESQER MCAVVSPKNV DAFLAVCRKW
EVLATVIGEV TDGDRLQITW HGETVVDVPP RTVAHEGPVY QRPVARPDTQ DALNADRSAK
LSRPVTGDEL RATLLALLGS PHLCSRAFIT EQYDRYVRGN TVLAEHADGG MLRIDQSTGR
GIAVSTDASG RYTLLDPYAG AQLALAEAYR NVAVTGATPV AVTNCLNFGS PEDPGVMWQF
TQAVRGLADG CADLGIPVTG GNVSFYNQTG SAAILPTPVV GVLGVIDDVR RRIPTGLGAE
PGETLMLLGD TRDEFDGSVW AQVTADHLGG LPPVVDLARE KLLAAVLSSA SRDGLVSAAH
DLSEGGLAQA IVESALAGET GCRIVLPEGA DPFVLLFSES AGRVLVAVPR TEESRFRGMC
EARGLPAVRI GVVDQGSDAV EVQGLFAVSL AELRATSEAV LPRYFG
