PUR1_BACSU
ID PUR1_BACSU Reviewed; 476 AA.
AC P00497;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:6794613};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE Flags: Precursor;
GN Name=purF {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000303|PubMed:6411717};
GN OrderedLocusNames=BSU06490;
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=6411717; DOI=10.1016/s0021-9258(17)44497-8;
RA Makaroff C.A., Zalkin H., Switzer R.L., Vollmer S.J.;
RT "Cloning of the Bacillus subtilis glutamine phosphoribosylpyrophosphate
RT amidotransferase gene in Escherichia coli. Nucleotide sequence
RT determination and properties of the plasmid-encoded enzyme.";
RL J. Biol. Chem. 258:10586-10593(1983).
RN [2]
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 [3]
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 [4]
RP SEQUENCE REVISION TO 413.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6794613; DOI=10.1021/bi00523a005;
RA Wong J.Y., Bernlohr D.A., Turnbough C.L., Switzer R.L.;
RT "Purification and properties of glutamine phosphoribosylpyrophosphate
RT amidotransferase from Bacillus subtilis.";
RL Biochemistry 20:5669-5674(1981).
RN [6]
RP ACTIVE SITE, AND PROTEIN SEQUENCE OF 12-35.
RX PubMed=6411716; DOI=10.1016/s0021-9258(17)44496-6;
RA Vollmer S.J., Switzer R.L., Hermodson M.A., Bower S.G., Zalkin H.;
RT "The glutamine-utilizing site of Bacillus subtilis glutamine
RT phosphoribosylpyrophosphate amidotransferase.";
RL J. Biol. Chem. 258:10582-10585(1983).
RN [7]
RP MUTAGENESIS OF CYS-12.
RX PubMed=6094545; DOI=10.1016/s0021-9258(18)89882-9;
RA Maentsaelae P., Zalkin H.;
RT "Glutamine amidotransferase function. Replacement of the active-site
RT cysteine in glutamine phosphoribosylpyrophosphate amidotransferase by site-
RT directed mutagenesis.";
RL J. Biol. Chem. 259:14230-14236(1984).
RN [8]
RP MUTAGENESIS.
RX PubMed=3090047; DOI=10.1016/s0021-9258(18)67401-0;
RA Makaroff C.A., Paluh J.L., Zalkin H.;
RT "Mutagenesis of ligands to the [4 Fe-4S] center of Bacillus subtilis
RT glutamine phosphoribosylpyrophosphate amidotransferase.";
RL J. Biol. Chem. 261:11416-11423(1986).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S),
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=8197456; DOI=10.1126/science.8197456;
RA Smith J.L., Zaluzec E.J., Wery J.-P., Niu L., Switzer R.L., Zalkin H.,
RA Satow Y.;
RT "Structure of the allosteric regulatory enzyme of purine biosynthesis.";
RL Science 264:1427-1433(1994).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S)
RP AND MAGNESIUM.
RX PubMed=9271502; DOI=10.1021/bi9711893;
RA Chen S., Tomchick D.R., Wolle D., Hu P., Smith J.L., Switzer R.L.,
RA Zalkin H.;
RT "Mechanism of the synergistic end-product regulation of Bacillus subtilis
RT glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides.";
RL Biochemistry 36:10718-10726(1997).
CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-
CC Rule:MF_01931, ECO:0000269|PubMed:6794613}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01931, ECO:0000269|PubMed:6794613};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01931,
CC ECO:0000269|PubMed:9271502};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01931,
CC ECO:0000269|PubMed:9271502};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:8197456};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The [4Fe-4S] cluster
CC requires a potential lower than -600 mV for reduction.
CC {ECO:0000269|PubMed:8197456};
CC -!- ACTIVITY REGULATION: Allosterically regulated; subject to end product
CC regulation by purine nucleotides. {ECO:0000269|PubMed:8197456}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01931}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8197456}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01931,
CC ECO:0000305}.
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DR EMBL; J02732; AAA22680.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12469.2; -; Genomic_DNA.
DR PIR; A00582; XQBS.
DR RefSeq; NP_388531.2; NC_000964.3.
DR RefSeq; WP_003233947.1; NZ_JNCM01000032.1.
DR PDB; 1AO0; X-ray; 2.80 A; A/B/C/D=12-470.
DR PDB; 1GPH; X-ray; 3.00 A; 1/2/3/4=12-476.
DR PDBsum; 1AO0; -.
DR PDBsum; 1GPH; -.
DR AlphaFoldDB; P00497; -.
DR SMR; P00497; -.
DR IntAct; P00497; 1.
DR MINT; P00497; -.
DR STRING; 224308.BSU06490; -.
DR DrugBank; DB01972; Guanosine-5'-Monophosphate.
DR MEROPS; C44.001; -.
DR PaxDb; P00497; -.
DR PRIDE; P00497; -.
DR EnsemblBacteria; CAB12469; CAB12469; BSU_06490.
DR GeneID; 936046; -.
DR KEGG; bsu:BSU06490; -.
DR PATRIC; fig|224308.179.peg.705; -.
DR eggNOG; COG0034; Bacteria.
DR InParanoid; P00497; -.
DR OMA; ENAQPTF; -.
DR PhylomeDB; P00497; -.
DR BioCyc; BSUB:BSU06490-MON; -.
DR BRENDA; 2.4.2.14; 658.
DR UniPathway; UPA00074; UER00124.
DR EvolutionaryTrace; P00497; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR CDD; cd00715; GPATase_N; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_01931; PurF; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005854; PurF.
DR InterPro; IPR035584; PurF_N.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01134; purF; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Allosteric enzyme; Direct protein sequencing;
KW Glutamine amidotransferase; Glycosyltransferase; Iron; Iron-sulfur;
KW Magnesium; Metal-binding; Purine biosynthesis; Reference proteome;
KW Transferase.
FT PROPEP 1..11
FT /evidence="ECO:0000269|PubMed:6411716"
FT /id="PRO_0000029251"
FT CHAIN 12..476
FT /note="Amidophosphoribosyltransferase"
FT /id="PRO_0000029252"
FT DOMAIN 12..231
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT ECO:0000269|PubMed:6411716"
FT BINDING 247
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT ECO:0000269|PubMed:8197456, ECO:0000269|PubMed:9271502"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT ECO:0000269|PubMed:9271502"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT ECO:0000269|PubMed:9271502"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT ECO:0000269|PubMed:9271502"
FT BINDING 393
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT ECO:0000269|PubMed:8197456, ECO:0000269|PubMed:9271502"
FT BINDING 448
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT ECO:0000269|PubMed:8197456, ECO:0000269|PubMed:9271502"
FT BINDING 451
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT ECO:0000269|PubMed:8197456, ECO:0000269|PubMed:9271502"
FT MUTAGEN 12
FT /note="C->F: Loss of enzyme activity and N-terminal
FT processing."
FT /evidence="ECO:0000269|PubMed:6094545"
FT MUTAGEN 394
FT /note="F->V: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:3090047"
FT MUTAGEN 442
FT /note="D->S: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:3090047"
FT MUTAGEN 448
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:3090047"
FT MUTAGEN 451
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:3090047"
FT MUTAGEN 452
FT /note="F->C: Lethal."
FT /evidence="ECO:0000269|PubMed:3090047"
FT CONFLICT 413
FT /note="E -> G (in Ref. 1 and 2; AAA22680)"
FT /evidence="ECO:0000305"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1GPH"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1GPH"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1AO0"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1GPH"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 266..281
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1AO0"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 351..357
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:1AO0"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:1AO0"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 412..419
FT /evidence="ECO:0007829|PDB:1AO0"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 429..436
FT /evidence="ECO:0007829|PDB:1AO0"
FT TURN 443..446
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:1AO0"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:1AO0"
SQ SEQUENCE 476 AA; 51692 MW; 6BC2FDA3288002F0 CRC64;
MLAEIKGLNE ECGVFGIWGH EEAPQITYYG LHSLQHRGQE GAGIVATDGE KLTAHKGQGL
ITEVFQNGEL SKVKGKGAIG HVRYATAGGG GYENVQPLLF RSQNNGSLAL AHNGNLVNAT
QLKQQLENQG SIFQTSSDTE VLAHLIKRSG HFTLKDQIKN SLSMLKGAYA FLIMTETEMI
VALDPNGLRP LSIGMMGDAY VVASETCAFD VVGATYLREV EPGEMLIIND EGMKSERFSM
NINRSICSME YIYFSRPDSN IDGINVHSAR KNLGKMLAQE SAVEADVVTG VPDSSISAAI
GYAEATGIPY ELGLIKNRYV GRTFIQPSQA LREQGVRMKL SAVRGVVEGK RVVMVDDSIV
RGTTSRRIVT MLREAGATEV HVKISSPPIA HPCFYGIDTS THEELIASSH SVEEIRQEIG
ADTLSFLSVE GLLKGIGRKY DDSNCGQCLA CFTGKYPTEI YQDTVLPHVK EAVLTK
