PURS_THEMA
ID PURS_THEMA Reviewed; 82 AA.
AC Q9X0X1; G4FEA4;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=TM_1244;
GN ORFNames=THEMA_08115, Tmari_1249;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RG DOE Joint Genome Institute;
RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
RX PubMed=16865708; DOI=10.1002/prot.21024;
RA Mathews I.I., Krishna S.S., Schwarzenbacher R., McMullan D.,
RA Jaroszewski L., Miller M.D., Abdubek P., Agarwalla S., Ambing E.,
RA Axelrod H.L., Canaves J.M., Carlton D., Chiu H.J., Clayton T., DiDonato M.,
RA Duan L., Elsliger M.A., Grzechnik S.K., Hale J., Hampton E., Haugen J.,
RA Jin K.K., Klock H.E., Koesema E., Kovarik J.S., Kreusch A., Kuhn P.,
RA Levin I., Morse A.T., Nigoghossian E., Okach L., Oommachen S., Paulsen J.,
RA Quijano K., Reyes R., Rife C.L., Spraggon G., Stevens R.C.,
RA van den Bedem H., White A., Wolf G., Xu Q., Hodgson K.O., Wooley J.,
RA Deacon A.M., Godzik A., Lesley S.A., Wilson I.A.;
RT "Crystal structure of phosphoribosylformyl-glycinamidine synthase II, PurS
RT subunit (TM1244) from Thermotoga maritima at 1.90 A resolution.";
RL Proteins 65:249-254(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=18597481; DOI=10.1021/bi800329p;
RA Morar M., Hoskins A.A., Stubbe J., Ealick S.E.;
RT "Formylglycinamide ribonucleotide amidotransferase from Thermotoga
RT maritima: structural insights into complex formation.";
RL Biochemistry 47:7816-7830(2008).
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, ECO:0000269|PubMed:18597481}.
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, ECO:0000269|PubMed:18597481};
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. {ECO:0000269|PubMed:16865708,
CC ECO:0000269|PubMed:18597481}.
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; AE000512; AAD36319.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL50173.1; -; Genomic_DNA.
DR EMBL; CP007013; AHD18851.1; -; Genomic_DNA.
DR PIR; F72276; F72276.
DR RefSeq; NP_229049.1; NC_000853.1.
DR RefSeq; WP_004080026.1; NZ_CP011107.1.
DR PDB; 1VQ3; X-ray; 1.90 A; A/B/C/D=1-82.
DR PDB; 3D54; X-ray; 3.50 A; B/C/F/G/J/K=1-82.
DR PDBsum; 1VQ3; -.
DR PDBsum; 3D54; -.
DR AlphaFoldDB; Q9X0X1; -.
DR SMR; Q9X0X1; -.
DR STRING; 243274.THEMA_08115; -.
DR EnsemblBacteria; AAD36319; AAD36319; TM_1244.
DR EnsemblBacteria; AGL50173; AGL50173; Tmari_1249.
DR KEGG; tma:TM1244; -.
DR KEGG; tmi:THEMA_08115; -.
DR KEGG; tmm:Tmari_1249; -.
DR KEGG; tmw:THMA_1269; -.
DR PATRIC; fig|243274.17.peg.1247; -.
DR eggNOG; COG1828; Bacteria.
DR InParanoid; Q9X0X1; -.
DR OMA; DIQYKSN; -.
DR OrthoDB; 2012814at2; -.
DR BRENDA; 6.3.5.3; 6331.
DR UniPathway; UPA00074; UER00128.
DR EvolutionaryTrace; Q9X0X1; -.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; 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..82
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurS"
FT /id="PRO_0000430099"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:1VQ3"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:1VQ3"
FT STRAND 36..50
FT /evidence="ECO:0007829|PDB:1VQ3"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:1VQ3"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1VQ3"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:1VQ3"
SQ SEQUENCE 82 AA; 9639 MW; 1B8470FFF1C78673 CRC64;
MPLFKFAIDV QYRSNVRDPR GETIERVLRE EKGLPVKKLR LGKSIHLEVE AENKEKAYEI
VKKACEELLV NPVVEEYEVR EL
