GenomeNet

Database: UniProt
Entry: F2I4I0_AERUA
LinkDB: F2I4I0_AERUA
Original site: F2I4I0_AERUA 
ID   F2I4I0_AERUA            Unreviewed;       227 AA.
AC   F2I4I0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
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   ECO:0000313|EMBL:AEA00295.1};
GN   OrderedLocusNames=HMPREF9243_0936 {ECO:0000313|EMBL:AEA00295.1};
OS   Aerococcus urinae (strain CCUG 59500 / ACS-120-V-Col10a).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus;
OC   Aerococcus incertae sedis.
OX   NCBI_TaxID=2976812 {ECO:0000313|EMBL:AEA00295.1, ECO:0000313|Proteomes:UP000008129};
RN   [1] {ECO:0000313|Proteomes:UP000008129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-120-V-Col10a {ECO:0000313|Proteomes:UP000008129};
RA   Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., Nelson K.E.;
RT   "Complete genome sequence of Aerococcus urinae strain ACS-120-V-Col10a.";
RL   Submitted (FEB-2011) 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}.
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; CP002512; AEA00295.1; -; Genomic_DNA.
DR   RefSeq; WP_013668554.1; NC_015278.1.
DR   AlphaFoldDB; F2I4I0; -.
DR   STRING; 866775.HMPREF9243_0936; -.
DR   KEGG; aur:HMPREF9243_0936; -.
DR   PATRIC; fig|866775.3.peg.887; -.
DR   eggNOG; COG0047; Bacteria.
DR   HOGENOM; CLU_001031_3_1_9; -.
DR   OMA; LHFVCRD; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000008129; 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|HAMAP-Rule:MF_00421};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00421};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00421};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00421, ECO:0000313|EMBL:AEA00295.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00421};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00421};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008129}.
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   227 AA;  24523 MW;  E2AD3396A90D38D6 CRC64;
     MKFAVIQFPG SNCDMDMLTA IRDILGQEAD YVPASATSLA GYDAIMLPGG FSFGDYLRTG
     AIARFTPIME EVKRLAQNGK LVLGTCNGFQ ILCESGLLPG SFLPNRDLTF ICKKQELMVE
     NNQSPFSSLY QEGEEITLPI AHGEGNYYCD EATLADLKAN GQIIFTYAGE NPNGSTGNIA
     GITNKAGNVI GLMPHPERAV EEIIAGQDGL KVFQSMVKYF ETAGKRA
//
DBGET integrated database retrieval system