(data stored in SCRATCH zone)

SWISSPROT: Q13S18_PARXL

ID   Q13S18_PARXL            Unreviewed;       516 AA.
AC   Q13S18;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 98.
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   ORFNames=Bxe_B2874 {ECO:0000313|EMBL:ABE33121.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33121.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33121.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33121.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000271; ABE33121.1; -; Genomic_DNA.
DR   RefSeq; WP_007178795.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_B2874; -.
DR   MEROPS; C44.001; -.
DR   EnsemblBacteria; ABE33121; ABE33121; Bxe_B2874.
DR   GeneID; 4006761; -.
DR   KEGG; bxb:DR64_5204; -.
DR   KEGG; bxe:Bxe_B2874; -.
DR   eggNOG; ENOG4105CBA; Bacteria.
DR   eggNOG; COG0034; LUCA.
DR   HOGENOM; HOG000033687; -.
DR   KO; K00764; -.
DR   OMA; FRPLCLG; -.
DR   OrthoDB; 267682at2; -.
DR   BioCyc; BXEN266265:BXE_RS22825-MONOMER; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000001817; Chromosome 2.
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; Q13S18.
DR   SWISS-2DPAGE; Q13S18.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
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:ABE33121.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:ABE33121.1}.
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   516 AA;  56347 MW;  7CFCF5701FDD58FC CRC64;
     MCGIVGVVSH SPVNQLIYDS LLLLQHRGQD AAGIATANGS NFHMHKANGM VRDVFRTRNM
     RSLPGTTGIG QVRYPTAGSA SSEEEAQPFY VNAPFGIILA HNGNLTNWQQ LKDEMFRIDR
     RHINTNSDTE VMLNVLAHEL QLSSSGLQLD PAALFNAVSG VHRRVRGSYA IVSLIAGYGL
     LGFRDPFGIR PLCLGKQETA EGVEWILASE SVAIEGIGFE FVRDVAPGEA IFIDLEGNLH
     SQQCATNPSL NPCIFELVYL ARPDSVLDGV PVYNVRLRMG DYLAEKIRRE LPDVAIDVVM
     PIPDSSRPAA MQVAKKLGVE YREGFFKNRY VGRTFIMPGQ AVRKKSVRQK LNAMGIEFKG
     KNVLIVDDSI VRGTTSHEIV QMARDAGANK VIFASAAPPV KFPNVYGIDM PTRGELVAHG
     RSDDEVARMI GADHLVYQDV DALKQAVRDI NPALKEFEAS CFDGNYVTGD VTTEYLDRIE
     TARLAPSSQS DRDAASEALD GGGPARSQLH LQLSVG
//

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