PURS_METJA
ID PURS_METJA Reviewed; 83 AA.
AC Q58988;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=MJ1593;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of Methanocaldococcus jannaschII purs, one of the
RT subunits of formylglycinamide ribonucleotide amidotransferase in the purine
RT biosynthetic pathway.";
RL Submitted (JUL-2011) to the PDB data bank.
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; L77117; AAB99611.1; -; Genomic_DNA.
DR PIR; H64498; H64498.
DR RefSeq; WP_010871117.1; NC_000909.1.
DR PDB; 2YX5; X-ray; 2.30 A; A=1-83.
DR PDBsum; 2YX5; -.
DR AlphaFoldDB; Q58988; -.
DR SMR; Q58988; -.
DR STRING; 243232.MJ_1593; -.
DR PRIDE; Q58988; -.
DR EnsemblBacteria; AAB99611; AAB99611; MJ_1593.
DR GeneID; 1452501; -.
DR KEGG; mja:MJ_1593; -.
DR eggNOG; arCOG04462; Archaea.
DR HOGENOM; CLU_164833_3_0_2; -.
DR InParanoid; Q58988; -.
DR OMA; PVIHDYE; -.
DR OrthoDB; 117509at2157; -.
DR PhylomeDB; Q58988; -.
DR BRENDA; 6.3.5.3; 3260.
DR UniPathway; UPA00074; UER00128.
DR EvolutionaryTrace; Q58988; -.
DR Proteomes; UP000000805; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..83
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurS"
FT /id="PRO_0000100399"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:2YX5"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:2YX5"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:2YX5"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:2YX5"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2YX5"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:2YX5"
SQ SEQUENCE 83 AA; 9696 MW; 461F8DDB0DF0B808 CRC64;
MYKATVIIKL KKGVLNPEGR TIQRALNFLG FNNVKEVQTY KMIDIIMEGE NEEKVKEEVE
EMCKKLLANP VIHDYEIKVE KIE
