GenomeNet

Database: UniProt
Entry: A0A0Q5E6G0_9MICO
LinkDB: A0A0Q5E6G0_9MICO
Original site: A0A0Q5E6G0_9MICO 
ID   A0A0Q5E6G0_9MICO        Unreviewed;       485 AA.
AC   A0A0Q5E6G0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=ASF68_07215 {ECO:0000313|EMBL:KQQ52155.1};
OS   Plantibacter sp. Leaf314.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Plantibacter.
OX   NCBI_TaxID=1736333 {ECO:0000313|EMBL:KQQ52155.1, ECO:0000313|Proteomes:UP000051200};
RN   [1] {ECO:0000313|EMBL:KQQ52155.1, ECO:0000313|Proteomes:UP000051200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52155.1,
RC   ECO:0000313|Proteomes:UP000051200};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ52155.1, ECO:0000313|Proteomes:UP000051200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52155.1,
RC   ECO:0000313|Proteomes:UP000051200};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC       phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-
CC       Rule:MF_01931}.
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:0000256|HAMAP-
CC         Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01931,
CC         ECO:0000256|PIRSR:PIRSR000485-2};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01931,
CC       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       ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00010138,
CC       ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01931}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQQ52155.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMOB01000001; KQQ52155.1; -; Genomic_DNA.
DR   RefSeq; WP_056008709.1; NZ_LMOB01000001.1.
DR   AlphaFoldDB; A0A0Q5E6G0; -.
DR   STRING; 1736333.ASF68_07215; -.
DR   OrthoDB; 9801213at2; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000051200; Unassembled WGS sequence.
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: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   Pfam; PF00156; Pribosyltran; 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   ECO:0000256|HAMAP-Rule:MF_01931};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_01931};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-
KW   2};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRSR:PIRSR000485-2};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01931}; Reference proteome {ECO:0000313|Proteomes:UP000051200};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01931}.
FT   DOMAIN          2..237
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   ACT_SITE        2
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT                   ECO:0000256|PIRSR:PIRSR000485-1"
FT   BINDING         306
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT                   ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         368
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT                   ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         369
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT                   ECO:0000256|PIRSR:PIRSR000485-2"
SQ   SEQUENCE   485 AA;  53241 MW;  6DC0859B91777B31 CRC64;
     MCGIVGIVST EPANQQVYDS LLLLQHRGQD STGIATADGS TFHMVKAKGQ VREAFRTRDM
     RSLLGNMGLG HVRYATKGDA ANESEAQPFY VNAPYGITLI HNGNLTNTRE LSKDLFHVDR
     RHVNSTSDTE LLLNVLATEL QGQISGLDLD PDQVFNAVEN VHERVEGSYA TIALIAGHGL
     LAFRDPFGIR PLILGKRQTG LVGNDWVVAS ESLVLEAGGY ETVREIAPGE AVFITASGEL
     YSRQCAKNPR LVPCSFEYVY LARPDSVMNG ISVYEARLRL GNRLADTIAE YTPMGDIDVV
     MPIPDSSRPA AMQVAQKLGI EYREGFYKNR YVGRTFIMPG QAQRKKSVRQ KLNAMGSEFK
     GKNILIVDDS IVRGTTSKEI VDMARLAGAN KVTFTSAAPP VRYPHVYGIN MPSRQELVAH
     GKKIPDIARE LGADNLIYQE VADMKAAILE GSGISDLEMS CFTGEYVTGT VSEEYLEWVE
     RSQLS
//
DBGET integrated database retrieval system