PURL_META3
ID PURL_META3 Reviewed; 732 AA.
AC A6UX13;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Maeo_1459;
OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS Nankai-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=419665;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL Submitted (JUN-2007) 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; CP000743; ABR57035.1; -; Genomic_DNA.
DR RefSeq; WP_011974167.1; NC_009635.1.
DR AlphaFoldDB; A6UX13; -.
DR SMR; A6UX13; -.
DR STRING; 419665.Maeo_1459; -.
DR EnsemblBacteria; ABR57035; ABR57035; Maeo_1459.
DR GeneID; 5326931; -.
DR KEGG; mae:Maeo_1459; -.
DR eggNOG; arCOG00641; Archaea.
DR HOGENOM; CLU_003100_0_1_2; -.
DR OMA; FIEPYQG; -.
DR OrthoDB; 860at2157; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001106; 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; Reference proteome.
FT CHAIN 1..732
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurL"
FT /id="PRO_1000050320"
FT ACT_SITE 32
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT ACT_SITE 83
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 82..85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 302..304
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 523
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 525
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
SQ SEQUENCE 732 AA; 79929 MW; 8344EDA36F1511AC CRC64;
MDLNDLKFIE EQLGRKPNDV EIGMFENLWS EHCSYRSTKK LLSMFGKTVK ENQNIVVGPG
DDAALIKIDD ETDLCVAMAM ESHNHPSYID PYNGAATGVG GIVRDIISMN AKPIALLNAL
RFGDINGEEK DKVRWLVEGV VDGIRDYGNR IGVPNVGGEC EFDKSYDYNN LVNVVCIGLV
KEGDIVTGKA KETDLTLILV GSTGRDGIGG ASFASKDLTS ESEGDRPSVQ IGDAFTEKCV
IDSTLEACAT KKVKAIKDLG AAGITSSCSE LCYSGGVGAE LYLENVILRD EGMTAYEIMV
SESQERMLLA VEKGSEEEII KIFEKYELPV SIIGKTTDTK RFFVKMNDEV VVDLPLDLLC
EATLTDSEEK ETILETPDNK ENIAEPEPAE LNNILLKLLK SPNINSKKWI YEQYDHEVQL
NTVVRPGKDA SVLRLKEAHP KALALVADCN PTYCKLNPYG GSLNLVCESV RNLATVGAKP
IGMLDNLNFG NPEKPERFYQ IKKCIEGLAD GAEIIGVPVV GGNVSLYNET VIDGKDYPIN
PTPVISIVGT IENINNIPKG AKEGDILIIT APTKDEMGGT EYYKQIHNTE EGIVPKANLE
VEKEIYSKVC ELVNNGLINE AVDCSKGGLG VAISKLCMTN NIGVELDLGD YNTNGLRNDI
LLFSESSGRI ILSVDKNNAD KVVKELNGAI IGTVKGNELK IKLNDNELIN LPIEEMKNKY
ENAFSEMMGE NI
