ID A4J724_DESRM Unreviewed; 233 AA.
AC A4J724;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurQ {ECO:0000256|HAMAP-Rule:MF_00421};
DE Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00421};
DE EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00421};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit I {ECO:0000256|HAMAP-Rule:MF_00421};
DE Short=FGAR amidotransferase I {ECO:0000256|HAMAP-Rule:MF_00421};
DE Short=FGAR-AT I {ECO:0000256|HAMAP-Rule:MF_00421};
DE AltName: Full=Glutaminase PurQ {ECO:0000256|HAMAP-Rule:MF_00421};
DE EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_00421};
DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit I {ECO:0000256|HAMAP-Rule:MF_00421};
GN Name=purQ {ECO:0000256|HAMAP-Rule:MF_00421};
GN OrderedLocusNames=Dred_2367 {ECO:0000313|EMBL:ABO50877.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50877.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO50877.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50877.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-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:0000256|HAMAP-Rule:MF_00421}.
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_00421};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00421};
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_00421}.
CC -!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ
CC and 2 PurS subunits. {ECO:0000256|HAMAP-Rule:MF_00421}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00421}.
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DR EMBL; CP000612; ABO50877.1; -; Genomic_DNA.
DR RefSeq; WP_011878675.1; NC_009253.1.
DR AlphaFoldDB; A4J724; -.
DR STRING; 349161.Dred_2367; -.
DR KEGG; drm:Dred_2367; -.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_3_1_9; -.
DR OrthoDB; 9804441at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
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 GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00421; PurQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ.
DR NCBIfam; TIGR01737; FGAM_synth_I; 1.
DR PANTHER; PTHR47552; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ; 1.
DR PANTHER; PTHR47552:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ; 1.
DR Pfam; PF13507; GATase_5; 1.
DR PIRSF; PIRSF001586; FGAM_synth_I; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00421};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00421};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_00421};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00421};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00421};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00421};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00421}; Reference proteome {ECO:0000313|Proteomes:UP000001556}.
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 203
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 205
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 233 AA; 25452 MW; 584E063E2DEC2009 CRC64;
MKFGVVVFPG SNCDADCLHA IKTVTGQPVD YIWHKSGSVD GYDCIVLPGG FSYGDYLRCG
AVARFSPVMS PVIEFARRGG LVLGICNGFQ VLTEAGLLPG ALHRNKNLSF LCHDTYLRVE
NDISPFTSLA SRGSVIKVPI AHGEGNYFAD SDTVRRLEEN NQVVFRYCDY NGEITQGVNP
NGSVNNIAGI CNEQGNVLGM MPHPERCAEE ILGNIDGQLI FKSLLETWQR RCG
//
