PURS_BACSU
ID PURS_BACSU Reviewed; 84 AA.
AC P12049;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 140.
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}; Synonyms=yexA;
GN OrderedLocusNames=BSU06460;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3036807; DOI=10.1016/s0021-9258(18)47560-6;
RA Ebbole D.J., Zalkin H.;
RT "Cloning and characterization of a 12-gene cluster from Bacillus subtilis
RT encoding nine enzymes for de novo purine nucleotide synthesis.";
RL J. Biol. Chem. 262:8274-8287(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND NOMENCLATURE.
RX PubMed=10784038; DOI=10.1099/00221287-146-4-807;
RA Saxild H.H., Nygaard P.;
RT "The yexA gene product is required for phosphoribosylformylglycinamidine
RT synthetase activity in Bacillus subtilis.";
RL Microbiology 146:807-814(2000).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS
RP SPECTROMETRY.
RX PubMed=15301530; DOI=10.1021/bi049127h;
RA Hoskins A.A., Anand R., Ealick S.E., Stubbe J.;
RT "The formylglycinamide ribonucleotide amidotransferase complex from
RT Bacillus subtilis: metabolite-mediated complex formation.";
RL Biochemistry 43:10314-10327(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=15301532; DOI=10.1021/bi0491292;
RA Anand R., Hoskins A.A., Bennett E.M., Sintchak M.D., Stubbe J.,
RA Ealick S.E.;
RT "A model for the Bacillus subtilis formylglycinamide ribonucleotide
RT amidotransferase multiprotein complex.";
RL Biochemistry 43:10343-10352(2004).
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:10784038,
CC ECO:0000269|PubMed:15301530}.
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:15301530};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=181 uM for ATP (at pH 7.2 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:15301530};
CC KM=507 uM for FGAR (at pH 7.2 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:15301530};
CC KM=1.3 mM for glutamine (at pH 7.2 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:15301530};
CC Note=kcat is 2.49 sec(-1) for FGAM synthase activity (at pH 7.2 and
CC 37 degrees Celsius).;
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 or homotetramer. Part of the FGAM synthase complex
CC composed of 1 PurL, 1 PurQ and 2 PurS subunits.
CC {ECO:0000269|PubMed:15301532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01926}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a purine auxotrophic
CC phenotype and an accumulation of FGAR due to defective FGAM synthetase
CC activity. {ECO:0000269|PubMed:10784038}.
CC -!- SIMILARITY: Belongs to the PurS family. {ECO:0000255|HAMAP-
CC Rule:MF_01926}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL009126; CAB12466.1; -; Genomic_DNA.
DR PIR; E29326; E29326.
DR RefSeq; NP_388528.1; NC_000964.3.
DR RefSeq; WP_003219409.1; NZ_JNCM01000032.1.
DR PDB; 1T4A; X-ray; 2.00 A; A/B=1-84.
DR PDB; 1TWJ; X-ray; 2.50 A; A/B/C/D=1-84.
DR PDBsum; 1T4A; -.
DR PDBsum; 1TWJ; -.
DR AlphaFoldDB; P12049; -.
DR SMR; P12049; -.
DR STRING; 224308.BSU06460; -.
DR PaxDb; P12049; -.
DR EnsemblBacteria; CAB12466; CAB12466; BSU_06460.
DR GeneID; 64302508; -.
DR GeneID; 936041; -.
DR KEGG; bsu:BSU06460; -.
DR PATRIC; fig|224308.179.peg.702; -.
DR eggNOG; COG1828; Bacteria.
DR InParanoid; P12049; -.
DR OMA; IENYRFE; -.
DR PhylomeDB; P12049; -.
DR BioCyc; BSUB:BSU06460-MON; -.
DR BioCyc; MetaCyc:BSU06460-MON; -.
DR UniPathway; UPA00074; UER00128.
DR EvolutionaryTrace; P12049; -.
DR Proteomes; UP000001570; 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_0000100395"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1T4A"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:1T4A"
FT STRAND 34..47
FT /evidence="ECO:0007829|PDB:1T4A"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:1T4A"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1T4A"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:1T4A"
SQ SEQUENCE 84 AA; 9755 MW; E7CD0BF1BB8874DD CRC64;
MYKVKVYVSL KESVLDPQGS AVQHALHSMT YNEVQDVRIG KYMELTIEKS DRDLDVLVKE
MCEKLLANTV IEDYRYEVEE VVAQ
