ID K6WQS5_9ACTN Unreviewed; 226 AA.
AC K6WQS5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:GAB88879.1};
GN ORFNames=GORHZ_046_00290 {ECO:0000313|EMBL:GAB88879.1};
OS Gordonia rhizosphera NBRC 16068.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1108045 {ECO:0000313|EMBL:GAB88879.1, ECO:0000313|Proteomes:UP000008363};
RN [1] {ECO:0000313|EMBL:GAB88879.1, ECO:0000313|Proteomes:UP000008363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16068 {ECO:0000313|EMBL:GAB88879.1,
RC ECO:0000313|Proteomes:UP000008363};
RA Takarada H., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA Ohji S., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia rhizosphera NBRC 16068.";
RL Submitted (AUG-2012) 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:GAB88879.1}.
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DR EMBL; BAHC01000046; GAB88879.1; -; Genomic_DNA.
DR RefSeq; WP_006330586.1; NZ_BAHC01000046.1.
DR AlphaFoldDB; K6WQS5; -.
DR STRING; 1108045.GORHZ_046_00290; -.
DR eggNOG; COG0047; Bacteria.
DR OrthoDB; 9804441at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000008363; 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|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:UP000008363}.
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 196
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 198
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 226 AA; 23662 MW; 18F30E3F8E5AF6D2 CRC64;
MTARIGVITF PGTLDDVDAV RAARLAGAEA VELWHGDADL KGVDAVIVPG GFSYGDYLRA
GAIARFAPVM GSVVEAAGKG MPVLGICNGF QVLCEAGLLP GALTRNEGLH FICRDEWLKV
ESNTTTWTSR FERGAEILIP LKSGEGRFVA PQRKLEELEG EGHIVFTYAG GNPNGSALDI
AGISSPDGRI VGLMPHPEHA TEALTGPSDD GLGLFYSVID SVLASA
//
