GenomeNet

Database: UniProt
Entry: A0A0R2RWD8_9PROT
LinkDB: A0A0R2RWD8_9PROT
Original site: A0A0R2RWD8_9PROT 
ID   A0A0R2RWD8_9PROT        Unreviewed;       227 AA.
AC   A0A0R2RWD8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ORFNames=ABS03_00800 {ECO:0000313|EMBL:KRO64893.1};
OS   Pelagibacteraceae bacterium BACL5 MAG-120820-bin39.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae.
OX   NCBI_TaxID=1655605 {ECO:0000313|EMBL:KRO64893.1, ECO:0000313|Proteomes:UP000051468};
RN   [1] {ECO:0000313|EMBL:KRO64893.1, ECO:0000313|Proteomes:UP000051468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL5 MAG-120820-bin39 {ECO:0000313|EMBL:KRO64893.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRO64893.1}.
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; LIBV01000023; KRO64893.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2RWD8; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000051468; Unassembled WGS sequence.
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};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00421};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00421}.
FT   ACT_SITE        85
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        201
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"
SQ   SEQUENCE   227 AA;  25579 MW;  F2E31F2ED89387D7 CRC64;
     MKSSVITFPG SNCDRDMDVA LKKFGFKNKM VWHNDVEIPK SDLVVLPGGF SYGDYLRCGS
     MASKSKIMNS VINFAKSGGL VLGVCNGFQI LVEAGLVPGV LLRNKYLEFI CKNVFVKIKN
     KENKYFRNLD KDILELHIAH NEGNYFCTKD QLKEINDNEQ IAIYYCNENG DIKEQYNPNG
     SIKNIAGIFS KEKNVLGMMP HPERMIDISL SGEDGSLFFN NLINNLK
//
DBGET integrated database retrieval system