ID U7MVB3_9CORY Unreviewed; 226 AA.
AC U7MVB3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=HMPREF1290_00234 {ECO:0000313|EMBL:ERS75168.1};
OS Corynebacterium sp. KPL1989.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1203622 {ECO:0000313|EMBL:ERS75168.1, ECO:0000313|Proteomes:UP000017102};
RN [1] {ECO:0000313|EMBL:ERS75168.1, ECO:0000313|Proteomes:UP000017102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KPL1989 {ECO:0000313|EMBL:ERS75168.1,
RC ECO:0000313|Proteomes:UP000017102};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K.,
RA Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Corynebacterium sp. KPL1989.";
RL Submitted (OCT-2013) 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:ERS75168.1}.
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DR EMBL; AXLR01000001; ERS75168.1; -; Genomic_DNA.
DR RefSeq; WP_021354014.1; NZ_KI515716.1.
DR AlphaFoldDB; U7MVB3; -.
DR GeneID; 42781883; -.
DR PATRIC; fig|1203622.3.peg.221; -.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_3_1_11; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000017102; 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:UP000017102}.
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 195
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 197
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 226 AA; 23891 MW; 9E0344E67A1BD894 CRC64;
MSPTIGVITF PGSLDDVDAA RAARLAGANV VELWHDDNSL HNVDGVIVPG GFSYGDYLRS
GAISALSPVM QAVIPAAREG MPTLGICNGF QILTESGLLP GALTRNQHLH FHCVDTYLEV
ANANTAWTSE YEQGQKILIP AKHGEGRFQA DAATIEQLEA EGRVVFRYTD NFNGSINSIA
GITNEAGNVV GLMPHPEHAV EALTGPSVDG LGIFRSALNA LSAEKL
//
