ID E1RHQ2_METP4 Unreviewed; 690 AA.
AC E1RHQ2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00420};
DE EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00420};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
DE Short=FGAR amidotransferase II {ECO:0000256|HAMAP-Rule:MF_00420};
DE Short=FGAR-AT II {ECO:0000256|HAMAP-Rule:MF_00420};
DE AltName: Full=Glutamine amidotransferase PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
GN Name=purL {ECO:0000256|HAMAP-Rule:MF_00420};
GN OrderedLocusNames=Mpet_0587 {ECO:0000313|EMBL:ADN35361.1};
OS Methanolacinia petrolearia (strain DSM 11571 / OCM 486 / SEBR 4847)
OS (Methanoplanus petrolearius).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanolacinia.
OX NCBI_TaxID=679926 {ECO:0000313|EMBL:ADN35361.1, ECO:0000313|Proteomes:UP000006565};
RN [1] {ECO:0000313|EMBL:ADN35361.1, ECO:0000313|Proteomes:UP000006565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11571 / OCM 486 / SEBR 4847
RC {ECO:0000313|Proteomes:UP000006565};
RX PubMed=21304750;
RA Brambilla E., Djao O.D., Daligault H., Lapidus A., Lucas S., Hammon N.,
RA Nolan M., Tice H., Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Spring S., Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Methanoplanus petrolearius type strain (SEBR
RT 4847).";
RL Stand. Genomic Sci. 3:203-211(2010).
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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00420}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420}.
CC -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000256|HAMAP-
CC Rule:MF_00420}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00420}.
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DR EMBL; CP002117; ADN35361.1; -; Genomic_DNA.
DR RefSeq; WP_013328539.1; NC_014507.1.
DR AlphaFoldDB; E1RHQ2; -.
DR STRING; 679926.Mpet_0587; -.
DR GeneID; 9743036; -.
DR KEGG; mpi:Mpet_0587; -.
DR eggNOG; arCOG00641; Archaea.
DR HOGENOM; CLU_003100_0_1_2; -.
DR OrthoDB; 8251at2157; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000006565; 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 CDD; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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 NCBIfam; TIGR01736; FGAM_synth_II; 1.
DR PANTHER; PTHR43555; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR PANTHER; PTHR43555:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR Pfam; PF00586; AIRS; 2.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR PIRSF; PIRSF001587; FGAM_synthase_II; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00420};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00420};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00420};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00420}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00420}; Reference proteome {ECO:0000313|Proteomes:UP000006565}.
FT DOMAIN 5..36
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 58..173
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 185..337
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 416..531
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT ACT_SITE 33
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT ACT_SITE 79
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 78..81
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 295..297
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 506
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 509
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
SQ SEQUENCE 690 AA; 74382 MW; 419D69F46831F906 CRC64;
MLSPCDEEYI EKKLGRKLTA LEYACFENLW SEHCSYRSTK PLLRTLPTDG ENVLLGPGDD
AAIVKFSDDI ALSIGMESHN HPSYVDPYDG AATGVGGIVR DIISMGSRPI ALMDPLFFGE
ISGEKNRYIF EHVVAGIGDY GNCIGVPVVR GDLVFDKKYA GNPLVNVVCV GIVHPDKFLT
ARVKQPGSRL ILYGSSTGRD GLGGASFASR DLSEDSEAED RPAVQVGDPY TEKLLIEATL
EIAETGKILS CRDLGAAGLA GASSEMSETF GARLYADRVH LREENMNEVE IFLAESQERM
LVEVRPEDVA EITSIIEKYD LKWSDIGEVT EEKKYVISFN GEIVCDLPID LLVGGAPEET
WSGSSYNVTK EYTKPRTPLK ELCLKVLSHP EIAKKDWVSR QYDHDVQLRS VSVGGGAACL
KLGDAGLYLS CGCSPRQIFL KPYEGTANAV YENAANLAAM GAEPLCIVNC LNFASPVHDD
VFWQISESVR GMGDMCRSLG VPVVGGNVSL YNESDEFGTQ IPPTPCIGMV GKGDVKIYKP
ATAGQKLALI GKCKSGMGGS LLDEITGCGG EAPAIPDTSV LEQVRSLVNN GRVSSATDVS
HGGLLAAVVS FAGTADLKLS GDPVETLFSE SYGRFLVAVE DEKTLEGIEY EILGTAGGHA
LKIRFENEDL VLEKDEIESA LDSTTKIMRY
//
