(data stored in SCRATCH zone)

SWISSPROT: Q47TM0_THEFY

ID   Q47TM0_THEFY            Unreviewed;       235 AA.
AC   Q47TM0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 106.
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   OrderedLocusNames=Tfu_0156 {ECO:0000313|EMBL:AAZ54194.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54194.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC       complex involved in the purines biosynthetic pathway. Catalyzes
CC       the ATP-dependent conversion of formylglycinamide ribonucleotide
CC       (FGAR) and glutamine to yield formylglycinamidine ribonucleotide
CC       (FGAM) and glutamate. The FGAM synthase complex is composed of
CC       three subunits. PurQ produces an ammonia molecule by converting
CC       glutamine to glutamate. PurL transfers the ammonia molecule to
CC       FGAR to form FGAM in an ATP-dependent manner. PurS interacts with
CC       PurQ and PurL and is thought to assist in the transfer of the
CC       ammonia molecule from PurQ to PurL. {ECO:0000256|HAMAP-
CC       Rule:MF_00421, ECO:0000256|SAAS:SAAS00064615}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-D-
CC         ribosyl)glycinamide = 2-(formamido)-N(1)-(5-phospho-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:58426, ChEBI:CHEBI:58478,
CC         ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00421, ECO:0000256|SAAS:SAAS01122701};
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         ECO:0000256|SAAS:SAAS01122695};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-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, ECO:0000256|SAAS:SAAS00064607}.
CC   -!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1
CC       PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-Rule:MF_00421,
CC       ECO:0000256|SAAS:SAAS00064604}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00421,
CC       ECO:0000256|SAAS:SAAS00371042}.
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DR   EMBL; CP000088; AAZ54194.1; -; Genomic_DNA.
DR   RefSeq; WP_011290603.1; NC_007333.1.
DR   STRING; 269800.Tfu_0156; -.
DR   EnsemblBacteria; AAZ54194; AAZ54194; Tfu_0156.
DR   KEGG; tfu:Tfu_0156; -.
DR   eggNOG; ENOG4105D21; Bacteria.
DR   eggNOG; COG0047; LUCA.
DR   HOGENOM; HOG000238240; -.
DR   KO; K01952; -.
DR   OMA; NCDRDVA; -.
DR   OrthoDB; 1527083at2; -.
DR   BioCyc; TFUS269800:G1G4Q-159-MONOMER; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000000434; 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   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00421; PurQ; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ.
DR   PIRSF; PIRSF001586; FGAM_synth_I; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01737; FGAM_synth_I; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TM0.
DR   SWISS-2DPAGE; Q47TM0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00448468};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00448436};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|PROSITE-ProRule:PRU00605, ECO:0000256|SAAS:SAAS00448451};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00064595};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00448458, ECO:0000313|EMBL:AAZ54194.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00448475};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00421,
KW   ECO:0000256|SAAS:SAAS00448464};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   DOMAIN        5    230       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   ACT_SITE     89     89       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00421, ECO:0000256|PROSITE-ProRule:
FT                                PRU00605}.
FT   ACT_SITE    198    198       {ECO:0000256|HAMAP-Rule:MF_00421,
FT                                ECO:0000256|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    200    200       {ECO:0000256|HAMAP-Rule:MF_00421,
FT                                ECO:0000256|PROSITE-ProRule:PRU00605}.
SQ   SEQUENCE   235 AA;  24825 MW;  B82E3D5864BA20D2 CRC64;
     MAAPRVGVVT FPGSLDDRDA ARAVRIAGAE PVSLWHGDAD LKGVDAVVLP GGFSYGDYLR
     CGAIARFAPI MTEIVPAARS GNLPVLGICN GFQILCESQL LPGALTRNAS RHFICRDQLI
     RVEAADTVWT NGYSPGQELL IPLKSGEGNY VADPETIAEL KRDNRVVVRY VDSAPNGSMD
     NIAGVTNEHR NVVGLMPHPE HAVEALTGPS TDGLGFFTSL LAHLTGSTPV PETAG
//

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