(data stored in ACNUC7421 zone)

SWISSPROT: Q47TJ8_THEFY

ID   Q47TJ8_THEFY            Unreviewed;        80 AA.
AC   Q47TJ8;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurS {ECO:0000256|HAMAP-Rule:MF_01926};
DE            Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_01926};
DE            EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_01926};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit III {ECO:0000256|HAMAP-Rule:MF_01926};
DE            Short=FGAR amidotransferase III {ECO:0000256|HAMAP-Rule:MF_01926};
DE            Short=FGAR-AT III {ECO:0000256|HAMAP-Rule:MF_01926};
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit III {ECO:0000256|HAMAP-Rule:MF_01926};
GN   Name=purS {ECO:0000256|HAMAP-Rule:MF_01926};
GN   OrderedLocusNames=Tfu_0178 {ECO:0000313|EMBL:AAZ54216.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54216.1, 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_01926}.
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_01926};
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_01926}.
CC   -!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1
CC       PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-Rule:MF_01926}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01926}.
CC   -!- SIMILARITY: Belongs to the PurS family. {ECO:0000256|HAMAP-
CC       Rule:MF_01926}.
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DR   EMBL; CP000088; AAZ54216.1; -; Genomic_DNA.
DR   RefSeq; WP_011290625.1; NC_007333.1.
DR   STRING; 269800.Tfu_0178; -.
DR   EnsemblBacteria; AAZ54216; AAZ54216; Tfu_0178.
DR   KEGG; tfu:Tfu_0178; -.
DR   eggNOG; ENOG4105VR9; Bacteria.
DR   eggNOG; COG1828; LUCA.
DR   HOGENOM; HOG000033801; -.
DR   KO; K01952; -.
DR   OMA; IENYRFE; -.
DR   OrthoDB; 2012814at2; -.
DR   BioCyc; TFUS269800:G1G4Q-181-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-UniRule.
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   Gene3D; 3.30.1280.10; -; 1.
DR   HAMAP; MF_01926; PurS; 1.
DR   InterPro; IPR003850; PurS.
DR   InterPro; IPR036604; PurS-like_sf.
DR   PANTHER; PTHR34696; PTHR34696; 1.
DR   Pfam; PF02700; PurS; 1.
DR   ProDom; PD010362; FGAM_PurS; 1.
DR   SUPFAM; SSF82697; SSF82697; 1.
DR   TIGRFAMs; TIGR00302; TIGR00302; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TJ8.
DR   SWISS-2DPAGE; Q47TJ8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01926};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01926};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01926};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01926};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01926};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
SQ   SEQUENCE   80 AA;  8879 MW;  D305CE03997082DA CRC64;
     MARVIVDVML KPEILDPQGQ AILGACERLG FSGVTQVRQG KRFEIDLEGE ADEARLAEIR
     KLAETLLANP VIEDFSLRVE
//

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