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Database: UniProt
Entry: S2WI36_9ACTN
LinkDB: S2WI36_9ACTN
Original site: S2WI36_9ACTN 
ID   S2WI36_9ACTN            Unreviewed;       225 AA.
AC   S2WI36;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=HMPREF9306_01826 {ECO:0000313|EMBL:EPD32257.1};
OS   Propionimicrobium lymphophilum ACS-093-V-SCH5.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionimicrobium.
OX   NCBI_TaxID=883161 {ECO:0000313|EMBL:EPD32257.1, ECO:0000313|Proteomes:UP000014417};
RN   [1] {ECO:0000313|EMBL:EPD32257.1, ECO:0000313|Proteomes:UP000014417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-093-V-SCH5 {ECO:0000313|EMBL:EPD32257.1,
RC   ECO:0000313|Proteomes:UP000014417};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Propionimicrobium lymphophilum ACS-093-V-SCH5.";
RL   Submitted (APR-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:EPD32257.1}.
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DR   EMBL; AGZR01000009; EPD32257.1; -; Genomic_DNA.
DR   RefSeq; WP_016456632.1; NZ_KE150269.1.
DR   AlphaFoldDB; S2WI36; -.
DR   STRING; 883161.HMPREF9306_01826; -.
DR   PATRIC; fig|883161.3.peg.1813; -.
DR   HOGENOM; CLU_001031_3_1_11; -.
DR   OrthoDB; 9804441at2; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000014417; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014417}.
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;  24508 MW;  88FE90428D0F137A CRC64;
     MTKIGVITFP GSLDDHDALR AIRLSGGTPV QLWHASDELG DVDAVVLPGG FSYGDYLRCG
     AIARFAPIMD ELIRQAKEGL PVLGICNGFQ MLCETHLLPG AMIRNESMKF ICRPERLRVE
     SVDTVWTCNF TPGQEIEIAL KNGEGNFQAD ADTVKRLEDN NQVVFRYLDN PNGSVNDIAG
     ITNERGNVVG LMPHPEHSVE TLTGSSTDGL GFFQSALAFL QRAAN
//
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