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
//