PURL_TRIV2
ID PURL_TRIV2 Reviewed; 777 AA.
AC Q3M6Z4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Ava_3636;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA23242.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3M6Z4; -.
DR SMR; Q3M6Z4; -.
DR STRING; 240292.Ava_3636; -.
DR EnsemblBacteria; ABA23242; ABA23242; Ava_3636.
DR KEGG; ava:Ava_3636; -.
DR eggNOG; COG0046; Bacteria.
DR HOGENOM; CLU_003100_0_1_3; -.
DR OMA; FIEPYQG; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002533; 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..777
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurL"
FT /id="PRO_0000236646"
FT ACT_SITE 50
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 95..98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 313..315
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 558
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 560
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
SQ SEQUENCE 777 AA; 83320 MW; D21EB57A49164600 CRC64;
MTATSPAPFS PQEIAAEGIK PEEYAEIVRR LGRHPNKAEL GMFGVMWSEH CCYKNSRPLL
KQFPTTGPRI LVGPGENAGV VDLGEGLQLA FKIESHNHPS AVEPFQGAAT GVGGILRDIF
TMGARPIALL NSLRFGSLED PKTQRLFSGV VAGISHYGNC VGVPTVGGEV YFDPAYSGNP
LVNVMALGLM ETPEIVKSGA SGIGNPVLYV GSTTGRDGMG GASFASAELS DESIDDRPAV
QVGDPFLEKS LIEACLEAFK TGAVVAAQDM GAAGITCSTS EMAAKGGVGI ELDLDKIPVR
ETGMIPYEYL LSESQERMLF VAHKGREQEL IDIFHRWGLQ AVVAGTVIAE PIVRILFQGA
IAAEIPADAL AENTPLYERE LLAEPPEYAR QAWEWSSDSL PTCTTAGIEI QGNLQSWQEI
LLTLLNTPTI ASKNWVYRQY DHQVQNNTVF LPGGADAAVV RLRPLEGQGK ITNTLSGVAA
TVDCNPRYVY LDPYEGAKAV VAEAARNLSC VGAEPLAVTD NLNFGSPEKP IGYWQLSEAC
RGLAEGCREL ATPVTGGNVS LYNETLDPQG NPQPIYPTPV VGMVGLITDL TKICGQGWQT
PGDVIYLLGA SITTLGASEY LATIHDTVAG RPPRVDFDLE RRVQKVCREG IYADWVRSAH
DCAEGGLVVA LAESCLAGNL GAEIHLDASG SQLQRLDEVL FGEGGARILV SVASTQQENW
ESYLQEHLGQ NWQKLGIVGN TDADLAVLTT DNQSLIRVSI EEMNDRYQNA IARRLAL
