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Phosphoribosylformylglycinamidine synthase subunit PurQ (FGAM synthase) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase subunit I) (FGAR amidotransferase I) (FGAR-AT I) (Glutaminase PurQ) (EC 3.5.1.2) (Phosphoribosylformylglycinamidine synthase subunit I)

 Q6UCP1_9PROT            Unreviewed;       223 AA.
Q6UCP1;
05-JUL-2004, integrated into UniProtKB/TrEMBL.
05-JUL-2004, sequence version 1.
27-SEP-2017, entry version 76.
RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurQ {ECO:0000256|HAMAP-Rule:MF_00421};
Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00421};
EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00421};
AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit I {ECO:0000256|HAMAP-Rule:MF_00421};
Short=FGAR amidotransferase I {ECO:0000256|HAMAP-Rule:MF_00421};
Short=FGAR-AT I {ECO:0000256|HAMAP-Rule:MF_00421};
AltName: Full=Glutaminase PurQ {ECO:0000256|HAMAP-Rule:MF_00421};
EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_00421};
AltName: Full=Phosphoribosylformylglycinamidine synthase subunit I {ECO:0000256|HAMAP-Rule:MF_00421};
Name=purQ {ECO:0000256|HAMAP-Rule:MF_00421};
ORFNames=HOT2C01.40 {ECO:0000313|EMBL:AAR05349.1};
uncultured marine alpha proteobacterium HOT2C01.
Bacteria; Proteobacteria; Alphaproteobacteria; environmental samples.
NCBI_TaxID=248049 {ECO:0000313|EMBL:AAR05349.1};
[1] {ECO:0000313|EMBL:AAR05349.1}
NUCLEOTIDE SEQUENCE.
PubMed=14566056; DOI=10.1073/pnas.2133554100;
De La Torre J.R., Christianson L.M., Beja O., Suzuki M.T., Karl D.M.,
Heidelberg J., DeLong E.F.;
"Proteorhodopsin genes are distributed among divergent marine
bacterial taxa.";
Proc. Natl. Acad. Sci. U.S.A. 100:12830-12835(2003).
[2] {ECO:0000313|EMBL:AAR05349.1}
NUCLEOTIDE SEQUENCE.
Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
complex involved in the purines biosynthetic pathway. Catalyzes
the ATP-dependent conversion of formylglycinamide ribonucleotide
(FGAR) and glutamine to yield formylglycinamidine ribonucleotide
(FGAM) and glutamate. The FGAM synthase complex is composed of
three subunits. PurQ produces an ammonia molecule by converting
glutamine to glutamate. PurL transfers the ammonia molecule to
FGAR to form FGAM in an ATP-dependent manner. PurS interacts with
PurQ and PurL and is thought to assist in the transfer of the
ammonia molecule from PurQ to PurL. {ECO:0000256|HAMAP-
Rule:MF_00421, ECO:0000256|SAAS:SAAS00371060}.
-!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D-
ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-
(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.
{ECO:0000256|HAMAP-Rule:MF_00421, ECO:0000256|SAAS:SAAS00371035}.
-!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3).
{ECO:0000256|HAMAP-Rule:MF_00421, ECO:0000256|SAAS:SAAS00064583}.
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000256|HAMAP-
Rule:MF_00421, ECO:0000256|SAAS:SAAS00371024}.
-!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1
PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-Rule:MF_00421,
ECO:0000256|SAAS:SAAS00371066}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00421,
ECO:0000256|SAAS:SAAS00371042}.
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EMBL; AY372455; AAR05349.1; -; Genomic_DNA.
ProteinModelPortal; Q6UCP1; -.
UniPathway; UPA00074; UER00128.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
Gene3D; 3.40.50.880; -; 1.
HAMAP; MF_00421; PurQ; 1.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR017926; GATASE.
InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ.
PIRSF; PIRSF001586; FGAM_synth_I; 1.
SUPFAM; SSF52317; SSF52317; 1.
TIGRFAMs; TIGR01737; FGAM_synth_I; 1.
PROSITE; PS51273; GATASE_TYPE_1; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00421,
ECO:0000256|SAAS:SAAS00064591};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00421,
ECO:0000256|SAAS:SAAS00064586};
Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00421,
ECO:0000256|SAAS:SAAS00064582};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_00421,
ECO:0000256|SAAS:SAAS00448455};
Ligase {ECO:0000256|HAMAP-Rule:MF_00421,
ECO:0000256|SAAS:SAAS00064592};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00421,
ECO:0000256|SAAS:SAAS00064591};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00421,
ECO:0000256|SAAS:SAAS00064605}.
DOMAIN 3 223 Glutamine amidotransferase type-1.
{ECO:0000259|PROSITE:PS51273}.
ACT_SITE 86 86 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_00421}.
ACT_SITE 200 200 {ECO:0000256|HAMAP-Rule:MF_00421}.
ACT_SITE 202 202 {ECO:0000256|HAMAP-Rule:MF_00421}.
SEQUENCE 223 AA; 24449 MW; D44A8919A72EBBC9 CRC64;
MKTHIIVFPG SNCDRDVAVA IKNISGHQPQ MVWHKETSIE KSDLIVVPGG FSYGDYLRCG
AMASTSPIMQ NVVKKANDGV PVMGICNGFQ ILIESGLLDG ALMRNKNLSF ICRDILIKPK
NTNSIFTKNA EVAKMPIAHN EGNYFANSEQ LKKIQDNDLI AFQYCDQAGN VDIQSNPNGS
LQNIAGILNE NKNVLGMMPH PERAAEMVHG CEDGKNIFES ILN


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