PURQ_BREBN
ID PURQ_BREBN Reviewed; 230 AA.
AC C0ZKC5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurQ {ECO:0000255|HAMAP-Rule:MF_00421};
DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00421};
DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00421};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit I {ECO:0000255|HAMAP-Rule:MF_00421};
DE Short=FGAR amidotransferase I {ECO:0000255|HAMAP-Rule:MF_00421};
DE Short=FGAR-AT I {ECO:0000255|HAMAP-Rule:MF_00421};
DE AltName: Full=Glutaminase PurQ {ECO:0000255|HAMAP-Rule:MF_00421};
DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00421};
DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit I {ECO:0000255|HAMAP-Rule:MF_00421};
GN Name=purQ {ECO:0000255|HAMAP-Rule:MF_00421}; OrderedLocusNames=BBR47_05990;
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599;
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) 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_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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00421}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00421}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008955; BAH41576.1; -; Genomic_DNA.
DR RefSeq; WP_012684342.1; NC_012491.1.
DR AlphaFoldDB; C0ZKC5; -.
DR SMR; C0ZKC5; -.
DR STRING; 358681.BBR47_05990; -.
DR EnsemblBacteria; BAH41576; BAH41576; BBR47_05990.
DR KEGG; bbe:BBR47_05990; -.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_3_1_9; -.
DR OMA; LHFVCRD; -.
DR OrthoDB; 1527083at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001877; 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-KW.
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 PIRSF; PIRSF001586; FGAM_synth_I; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01737; FGAM_synth_I; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glutamine amidotransferase; Hydrolase; Ligase;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..230
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurQ"
FT /id="PRO_1000134914"
FT DOMAIN 2..226
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 195
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
FT ACT_SITE 197
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00421"
SQ SEQUENCE 230 AA; 25563 MW; F06AAFE4A32C1862 CRC64;
MRVAVIVFPG SNADVDLFNA VEDVMGVPVD YVWHSDTDLS KYDAILLPGG FSYGDYLRCG
AVARFSPVME QVVKAADEGK LIMGICNGFQ ILTEVGLLPG ALLRNRSLKF RCKLSELRVE
NNDTSFTRDF AAGEVIQIPI AHGEGNYYCD EETLAKLKAN KQIVFRYHGE NPNGSLEDIA
GICNERGNVL GMMPHPERAV HSWMTSDDGR RMFTSILKTW REQNSVTTHA
