ID E6YZK5_BARSR Unreviewed; 222 AA.
AC E6YZK5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:CBI82293.1};
GN ORFNames=B11C_40148 {ECO:0000313|EMBL:CBI82293.1}, BscR1v2_008270
GN {ECO:0000313|EMBL:AQX30760.1};
OS Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=687861 {ECO:0000313|EMBL:CBI82293.1};
RN [1] {ECO:0000313|EMBL:CBI82293.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R1 {ECO:0000313|EMBL:CBI82293.1};
RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT "Parallel evolution of a type IV secretion system in radiating lineages of
RT the host-restricted bacterial pathogen Bartonella.";
RL PLoS Genet. 7:E1001296-E1001296(2011).
RN [2] {ECO:0000313|Proteomes:UP000190811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1 {ECO:0000313|Proteomes:UP000190811};
RX PubMed=28338931; DOI=10.1093/gbe/evx042;
RA Harms A., Segers F.H., Quebatte M., Mistl C., Manfredi P., Korner J.,
RA Chomel B.B., Kosoy M., Maruyama S., Engel P., Dehio C.;
RT "Evolutionary Dynamics of Pathoadaptation Revealed by Three Independent
RT Acquisitions of the VirB/D4 Type IV Secretion System in Bartonella.";
RL Genome Biol. Evol. 9:761-776(2017).
RN [3] {ECO:0000313|EMBL:AQX30760.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1 {ECO:0000313|EMBL:AQX30760.1};
RA Harms A., Segers F.H.I.D., Quebatte M., Mistl C., Manfredi P., Koerner J.,
RA Chomel B., Kosoy M., Maruyama S., Engel P., Dehio C.;
RT "Evolutionary dynamics of pathoadaptation revealed by three independent
RT acquisitions of the VirB/D4 type IV secretion system in Bartonella.";
RL Submitted (FEB-2017) 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; CP019789; AQX30760.1; -; Genomic_DNA.
DR EMBL; FN645509; CBI82293.1; -; Genomic_DNA.
DR AlphaFoldDB; E6YZK5; -.
DR STRING; 687861.BscR1v2_008270; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000190811; 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}.
FT ACT_SITE 86
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 222 AA; 24450 MW; 6E5438C97DCFC8B5 CRC64;
MKTAIIQLPG LNRDQDMIAA LYHITGIQPL KIWQTETTIP EVDMIVIPGG FSYGDYLRCG
AIGARMPVMQ AVHEKAQKGV MIMGVCNGFQ ILLESGLLPG ALMRNASLKF VCREIKLEVA
NADTKFSRCY SKGQIIRCPV AHHDGNYFVD NDTLKQMEDN KQIVFRYAEN TNPNGSINDI
AGIVNKTGNV LGIMPHPENF IETAHGGGDG RLLFQSVLES KN
//
