(data stored in SCRATCH zone)

SWISSPROT: Q7WA65_BORPA

ID   Q7WA65_BORPA            Unreviewed;       506 AA.
AC   Q7WA65;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 105.
DE   RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931};
DE            Short=ATase {ECO:0000256|HAMAP-Rule:MF_01931};
DE            EC=2.4.2.14 {ECO:0000256|HAMAP-Rule:MF_01931};
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
DE            Short=GPATase {ECO:0000256|HAMAP-Rule:MF_01931};
GN   Name=purF {ECO:0000256|HAMAP-Rule:MF_01931,
GN   ECO:0000313|EMBL:CAE36824.1};
GN   OrderedLocusNames=BPP1522 {ECO:0000313|EMBL:CAE36824.1};
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311 {ECO:0000313|Proteomes:UP000001421};
RN   [1] {ECO:0000313|Proteomes:UP000001421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC   {ECO:0000313|Proteomes:UP000001421};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.,
RA   Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.M., Temple L., James K., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC       phosphoribosylpyrophosphate (PRPP) and glutamine.
CC       {ECO:0000256|HAMAP-Rule:MF_01931}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
CC         = 5-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:0000256|HAMAP-
CC         Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-2};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-2};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_01931,
CC       ECO:0000256|PIRNR:PIRNR000485}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       purine/pyrimidine phosphoribosyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01931}.
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DR   EMBL; BX640427; CAE36824.1; -; Genomic_DNA.
DR   RefSeq; WP_010928075.1; NC_002928.3.
DR   MEROPS; C44.001; -.
DR   EnsemblBacteria; CAE36824; CAE36824; BPP1522.
DR   KEGG; bpa:BPP1522; -.
DR   HOGENOM; HOG000033687; -.
DR   KO; K00764; -.
DR   OMA; FRPLCLG; -.
DR   BioCyc; BPAR257311:G1GSY-1562-MONOMER; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
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:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   CDD; cd00715; GPATase_N; 1.
DR   CDD; cd06223; PRTases_typeI; 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   Pfam; PF00156; Pribosyltran; 1.
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.
PE   3: Inferred from homology;
DR   PRODOM; Q7WA65.
DR   SWISS-2DPAGE; Q7WA65.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001421};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:CAE36824.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRSR:PIRSR000485-2};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRSR:PIRSR000485-2};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRNR:PIRNR000485};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:CAE36824.1}.
FT   DOMAIN        2    236       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   ACT_SITE      2      2       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931, ECO:0000256|PIRSR:PIRSR000485-
FT                                1}.
FT   METAL       305    305       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931, ECO:0000256|PIRSR:PIRSR000485-
FT                                2}.
FT   METAL       367    367       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931, ECO:0000256|PIRSR:PIRSR000485-
FT                                2}.
FT   METAL       368    368       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931, ECO:0000256|PIRSR:PIRSR000485-
FT                                2}.
SQ   SEQUENCE   506 AA;  55555 MW;  06B69AAB0719EC81 CRC64;
     MCGIVGVIGR GPVNQLLYDS LLLLQHRGQD AAGIATLQGN HFNMYKAHGL VRDVFRTRNM
     RALPGTSGVG QVRYPTAGSS ASEEEAQPFY VNAPFGIMFA HNGNLTNWRE LRESLYRADR
     RHINTNSDSE VLLNVLAHEL QSAASGVSLD DDTIFRAVSA VHQRVKGAYA VVAQISGYGM
     LAFRDPHGIR PLCIGRQETE EGVEWMAASE SVALEGSGFA FVRDVEPGEA IFVDLDGRMT
     SRQCADNAQL VPCIFEYVYF ARPDSLIDGV SVYDARLRMG EYLADKVARS MRLGDIDVVM
     PIPDSSRPAA MQLAHRLGLD YREGLIKNRY VGRTFIMPGQ AVRRKSVRQK LNAIGMEFKG
     KNVLLVDDSI VRGTTSREIV DMARAAGANK VYFASAAPPV RFPNVYGIDM PTQKELIATG
     RTDDEIARTI GADALIYQDL QDMQQAVRDI NPRLSRFEAS CFDGEYVTGD ITAEYLARLG
     QSRDSSAGDE EAGGLQFNMG YAANDA
//

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