(data stored in SCRATCH zone)

SWISSPROT: A8LCH6_FRASN

ID   A8LCH6_FRASN            Unreviewed;        87 AA.
AC   A8LCH6;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 59.
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=Franean1_0148 {ECO:0000313|EMBL:ABW09615.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09615.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(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; CP000820; ABW09615.1; -; Genomic_DNA.
DR   STRING; 298653.Franean1_0148; -.
DR   EnsemblBacteria; ABW09615; ABW09615; Franean1_0148.
DR   KEGG; fre:Franean1_0148; -.
DR   eggNOG; ENOG410839H; Bacteria.
DR   eggNOG; COG1828; LUCA.
DR   HOGENOM; HOG000033801; -.
DR   KO; K01952; -.
DR   OMA; IENYRFE; -.
DR   BioCyc; FSP298653:G1G9X-146-MONOMER; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000001313; 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; A8LCH6.
DR   SWISS-2DPAGE; A8LCH6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01926};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
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:UP000001313}.
SQ   SEQUENCE   87 AA;  9389 MW;  8D79C2B3D0EA2D10 CRC64;
     MTRVVVDVML KPEILDPQGQ AVLTALPRLG VAGISGVRQG KRFELDLDGE ADAEALARIE
     HLASTLLANP VIEDYVVRVE PARVEAD
//

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