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Database: UniProt
Entry: N6UMV7_DENPD
LinkDB: N6UMV7_DENPD
Original site: N6UMV7_DENPD 
ID   N6UMV7_DENPD            Unreviewed;       486 AA.
AC   N6UMV7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|ARBA:ARBA00033770};
DE            EC=2.4.2.14 {ECO:0000256|ARBA:ARBA00011941};
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|ARBA:ARBA00033776};
DE   Flags: Fragment;
GN   ORFNames=YQE_01606 {ECO:0000313|EMBL:ENN82031.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ENN82031.1};
RN   [1] {ECO:0000313|EMBL:ENN82031.1, ECO:0000313|Proteomes:UP000019118}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
RN   [2] {ECO:0000313|EnsemblMetazoa:ENN82031}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JAN-2017) to UniProtKB.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00033607};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14907;
CC         Evidence={ECO:0000256|ARBA:ARBA00033607};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000485-2};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000485-2};
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:0000256|ARBA:ARBA00005209}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00010138}.
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DR   EMBL; APGK01017071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB739995; ENN82031.1; -; Genomic_DNA.
DR   AlphaFoldDB; N6UMV7; -.
DR   EnsemblMetazoa; ENN82031; ENN82031; YQE_01606.
DR   HOGENOM; CLU_022389_3_1_1; -.
DR   OMA; ENAQPTF; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000019118; Unassembled WGS sequence.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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; 3.40.50.2020; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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   NCBIfam; TIGR01134; purF; 1.
DR   PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000485-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000485-2};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          43..293
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   ACT_SITE        43
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-1"
FT   BINDING         359
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         421
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         422
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ENN82031.1"
SQ   SEQUENCE   486 AA;  53322 MW;  47B6E837F8FF8329 CRC64;
     MDTIEQRLAP TTSAVTYDVS EGSVGLMKRI KRGETLSGLT HECGVFGAIG TGEWPTHLEI
     SQIITWGLVA LQHRGQESAG IVTTEGRQSE NFNVVKGMGM VSNIFTDESI RKLKGSVGIG
     HTRYSTSAAS EEVNCQPFVV HTAHGPLAVA HNGELVNCDS LRRQVLEHGV GLSTHSDSEL
     ITQALCLNPP EGEPTGEPDW PARIRHFMQL APLSYSLVIM LRHKIYAIRD PYGNRPLCLG
     KILPFNEPIS GDCDEQRDAD GWVVSSESCG FLSIGAQYVR EVYPGEIIEM TRHGIRSIDI
     VHRPENKAQA FCIFEYVYFA RTDSIFEGQM VYAVRLQSGK QLAIEHPVEA DVVSAVPESG
     NAAAHGFSRQ SGISFAEVLC KNRYVGRSFI QPSNRLRKLL VAKKFGALAG MVKGKRIVLV
     DDSIVRGNTI GPIIKLLKNA GAIEVHIRIA SPPLQYPCYM GINIPTREEL IANKMNSREL
     AKHVGK
//
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