PURS_SYNY3
ID PURS_SYNY3 Reviewed; 100 AA.
AC Q55842;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurS {ECO:0000255|HAMAP-Rule:MF_01926};
DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_01926};
DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_01926};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit III {ECO:0000255|HAMAP-Rule:MF_01926};
DE Short=FGAR amidotransferase III {ECO:0000255|HAMAP-Rule:MF_01926};
DE Short=FGAR-AT III {ECO:0000255|HAMAP-Rule:MF_01926};
DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit III {ECO:0000255|HAMAP-Rule:MF_01926};
GN Name=purS {ECO:0000255|HAMAP-Rule:MF_01926}; OrderedLocusNames=slr0519;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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:0000255|HAMAP-Rule:MF_01926}.
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:0000255|HAMAP-
CC Rule:MF_01926};
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:0000255|HAMAP-
CC Rule:MF_01926}.
CC -!- SUBUNIT: Homodimer. Part of the FGAM synthase complex composed of 1
CC PurL, 1 PurQ and 2 PurS subunits (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01926}.
CC -!- SIMILARITY: Belongs to the PurS family. {ECO:0000255|HAMAP-
CC Rule:MF_01926}.
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DR EMBL; BA000022; BAA10598.1; -; Genomic_DNA.
DR PIR; S76654; S76654.
DR AlphaFoldDB; Q55842; -.
DR SMR; Q55842; -.
DR IntAct; Q55842; 3.
DR STRING; 1148.1001760; -.
DR PaxDb; Q55842; -.
DR EnsemblBacteria; BAA10598; BAA10598; BAA10598.
DR KEGG; syn:slr0519; -.
DR eggNOG; COG1828; Bacteria.
DR InParanoid; Q55842; -.
DR OMA; IENYRFE; -.
DR PhylomeDB; Q55842; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001425; 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 SUPFAM; SSF82697; SSF82697; 1.
DR TIGRFAMs; TIGR00302; TIGR00302; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..100
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurS"
FT /id="PRO_0000100397"
SQ SEQUENCE 100 AA; 10862 MW; 90AE2E11D7FAF8F7 CRC64;
MADSPVRPSM SHSYHCRIYV TLRPSVLDPA GTAVQSGLQQ LGYDGVSQVR IGKYIELTLE
APDEATASQQ LDTMCDQLLA NTVIENYCFE ITALEGAVTP
