GenomeNet

Database: UniProt
Entry: A0A0R1K9K8_9LACO
LinkDB: A0A0R1K9K8_9LACO
Original site: A0A0R1K9K8_9LACO 
ID   A0A0R1K9K8_9LACO        Unreviewed;       225 AA.
AC   A0A0R1K9K8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=FD03_GL000184 {ECO:0000313|EMBL:KRK80008.1};
OS   Companilactobacillus nodensis DSM 19682 = JCM 14932 = NBRC 107160.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Companilactobacillus.
OX   NCBI_TaxID=1423775 {ECO:0000313|EMBL:KRK80008.1, ECO:0000313|Proteomes:UP000051248};
RN   [1] {ECO:0000313|EMBL:KRK80008.1, ECO:0000313|Proteomes:UP000051248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19682 {ECO:0000313|EMBL:KRK80008.1,
RC   ECO:0000313|Proteomes:UP000051248};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRK80008.1}.
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; AZDZ01000009; KRK80008.1; -; Genomic_DNA.
DR   RefSeq; WP_025024061.1; NZ_BCWC01000007.1.
DR   AlphaFoldDB; A0A0R1K9K8; -.
DR   STRING; 1423775.FD03_GL000184; -.
DR   PATRIC; fig|1423775.4.peg.188; -.
DR   eggNOG; COG0047; Bacteria.
DR   OrthoDB; 9804441at2; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000051248; 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        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        194
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"
SQ   SEQUENCE   225 AA;  25175 MW;  2E961B0319C5B513 CRC64;
     MKFAVIVFPG SNCDMDLYYA IRDGIEQEAD LVSYKEESLD GYDGILIPGG FSYGDYLRSG
     AIASHAPIIK EVIRLANEGK PVLGICNGFQ ILTEIGLLPG TLTNNRQNRF ICKQVELVVE
     NNKTIFTNKY NLNEKIMVPI AHGEGRYYCD EETLWELNEN NQVVFRYSQD VNGSVEEIAG
     ITNKQKNVLG MMPHPERAIE SILGSDDGLK LFKSMLETQK NGVQI
//
DBGET integrated database retrieval system