PURS_METTH
ID PURS_METTH Reviewed; 84 AA.
AC O26271;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=MTH_169;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 1-81.
RX PubMed=12211007; DOI=10.1002/prot.10209;
RA Batra R., Christendat D., Edwards A., Arrowsmith C., Tong L.;
RT "Crystal structure of MTH169, a crucial component of
RT phosphoribosylformylglycinamidine synthetase.";
RL Proteins 49:285-288(2002).
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; AE000666; AAB84675.1; -; Genomic_DNA.
DR PIR; H69092; H69092.
DR RefSeq; WP_010875808.1; NC_000916.1.
DR PDB; 1GTD; X-ray; 2.56 A; A/B=1-81.
DR PDBsum; 1GTD; -.
DR AlphaFoldDB; O26271; -.
DR SMR; O26271; -.
DR STRING; 187420.MTH_169; -.
DR EnsemblBacteria; AAB84675; AAB84675; MTH_169.
DR GeneID; 1470130; -.
DR KEGG; mth:MTH_169; -.
DR PATRIC; fig|187420.15.peg.142; -.
DR HOGENOM; CLU_164833_3_0_2; -.
DR OMA; PVIHDYE; -.
DR UniPathway; UPA00074; UER00128.
DR EvolutionaryTrace; O26271; -.
DR Proteomes; UP000005223; 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..84
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurS"
FT /id="PRO_0000100400"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:1GTD"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:1GTD"
FT STRAND 35..47
FT /evidence="ECO:0007829|PDB:1GTD"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:1GTD"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1GTD"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:1GTD"
SQ SEQUENCE 84 AA; 9641 MW; 852F1BC119D06895 CRC64;
MKFMVEVRIR LKKGMLNPEA ATIERALALL GYEVEDTDTT DVITFTMDED SLEAVEREVE
DMCQRLLCNP VIHDYDVSIN EMEG
