ID A0A975GPU5_9BACT Unreviewed; 1012 AA.
AC A0A975GPU5;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 7.
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 ECO:0000313|EMBL:QTA89381.1};
GN ORFNames=dnm_054320 {ECO:0000313|EMBL:QTA89381.1};
OS Desulfonema magnum.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
OC Desulfobacterales; Desulfococcaceae; Desulfonema.
OX NCBI_TaxID=45655 {ECO:0000313|EMBL:QTA89381.1, ECO:0000313|Proteomes:UP000663722};
RN [1] {ECO:0000313|EMBL:QTA89381.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4be13 {ECO:0000313|EMBL:QTA89381.1};
RX PubMed=33611323; DOI=10.1159/000513383;
RA Schnaars V., Wohlbrand L., Scheve S., Hinrichs C., Reinhardt R., Rabus R.;
RT "Proteogenomic Insights into the Physiology of Marine, Sulfate-Reducing,
RT Filamentous Desulfonema limicola and Desulfonema magnum.";
RL Microb. Physiol. 0:1-20(2021).
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=N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + L-
CC glutamine + ATP + H2O = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + L-glutamate + ADP + phosphate + H(+);
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; CP061800; QTA89381.1; -; Genomic_DNA.
DR RefSeq; WP_207678028.1; NZ_CP061800.1.
DR AlphaFoldDB; A0A975GPU5; -.
DR KEGG; dmm:dnm_054320; -.
DR Proteomes; UP000663722; 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; 3.30.1280.10; Phosphoribosylformylglycinamidine synthase subunit PurS; 2.
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 InterPro; IPR036604; PurS-like_sf.
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; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR SUPFAM; SSF82697; PurS-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00420};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00420};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00420};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00420}; Reference proteome {ECO:0000313|Proteomes:UP000663722}.
FT DOMAIN 190..248
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 296..419
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 435..586
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 697..797
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 842..982
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 245
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 542..544
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 749
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 794
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 797
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
SQ SEQUENCE 1012 AA; 111289 MW; B250640377C976B9 CRC64;
MPYQLEITLK TDLFDAEGEG IRQKAENYFG IELAQVRTIR VLTIDVNLSA DHLEKIRTEI
FTNPVTDISS YAPLPVDFDW TIWVGYRPGV KDNPGSTAME AVEDILGIKT GPDEAIYTSK
RYCLKGDGLT AKDADMIAGE LLANDLIQQW KIIPQKQWNP KKGTGMIIPK VILNHEPTVT
SVPIDSDATL KKISDERNLA LNPNDIPIIR AYFLDKKVQA ERALAGLSEP TDIELEYISQ
ARSDHCNHNT FQGLFRYKEG ADGSVEIVDN LFETCIKAPT LELKEKKPWV VSVLWDNAGA
GRFDDDHYYV ITGETHNSPS NMEAYGGAIT GIVGVYRDPL GTGKGSKLVM GSYGFCVGPR
DYDGDLRPKL HPRRLLDGVI EGVRDGGNKS GIPTPFGQVL FHQGYMGKCL VFVTAVGIMP
ATVDGKPAEQ KTTSPGEMVI MCGGRVGKDG IHGVTASSEV FSENTPAGHV QIGDPYTQKK
MHDFLLEARD EGLIQFITDN GGGGLSSSVG ESALFSNGCE IQLEKVPLKY EGLDQWEIWI
SESQERMTVA VRPEDIQRFL SLSEKHAVES TVIGTYADSG KLHITYNGKT CAYVNLDLLK
SGFPQWEFDA EWLSPHDRGM TEPVLSEPRD YDRLLMDMLS RPNICSKEWI TRQYDHEVQG
TSVIKPLVGE DRDVNSDAAV ISKLETGNWK LETGNLKLET GGKGLAFSQA LLPAYSVIDA
YHMTSCTIDE AVRRLIAVGG NLEHIGGVDN FCWPNIQYHP ENNPDGKFKA AQLVRSCRAL
RDMCMAYEIP LLSGKDSMYV DGHLPGKYGE THKVSAPETL QFSCIGVIDD ITKCVTMDAK
IPGDLVYVLG ATRDELGASE YYEHFGHIGK NVPGVFPDQF IPVYKGLCHA IKEELVASVH
GIYRGGLGVH LAMVAMGGNI GMNVDLSLVP AEQVSRNDVI LFSESAGRFI VTIDPANRKK
FETIFKGMPC ACIGEITNGS DFIAKGIDKR TLLNVPVQQL KTAWKSPFAG LI
//
