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Database: UniProt
Entry: A0A0Q5I0K2_9BURK
LinkDB: A0A0Q5I0K2_9BURK
Original site: A0A0Q5I0K2_9BURK 
ID   A0A0Q5I0K2_9BURK        Unreviewed;       508 AA.
AC   A0A0Q5I0K2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=ASF77_00835 {ECO:0000313|EMBL:KQQ96583.1};
OS   Massilia sp. Leaf139.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ96583.1, ECO:0000313|Proteomes:UP000051760};
RN   [1] {ECO:0000313|EMBL:KQQ96583.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ96583.1,
RC   ECO:0000313|Proteomes:UP000051760};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ96583.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ96583.1,
RC   ECO:0000313|Proteomes:UP000051760};
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:KQQ96583.1}.
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DR   EMBL; LMOJ01000001; KQQ96583.1; -; Genomic_DNA.
DR   RefSeq; WP_056332980.1; NZ_LMOJ01000001.1.
DR   AlphaFoldDB; A0A0Q5I0K2; -.
DR   STRING; 1736272.ASF77_00835; -.
DR   OrthoDB; 9801213at2; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000051760; 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:UP000051760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01931}.
FT   DOMAIN          2..235
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         304
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         366
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         367
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   508 AA;  55562 MW;  8D4637F2256A8965 CRC64;
     MCGIVGVVSQ TPVNQLLYDA LLLLQHRGQD AAGIATNHSS MFSMYKANGL VRDVFRTRNM
     RSLQGNTGIG HCRYPTAGSS SEEEAQPFYV NAPFGITLAH NGNLTNQAEL KEALFRNDRR
     HINTNSDSEV LLNVLAHEVQ EAANGYSLDA EALFKAVGVV HKRVRGAYAV VAQIAGHGML
     AFRDPYGIRP LCLGMNEGEN GVEYMVASES VALEGIGFRF VRDIAPGEAV FIGDDGSFHE
     RQCAENPSLN PCAFEYVYLA RPDSVIDGAS VYATRLKMGE YLADKIRQEI PVEEIDVVMP
     IPDSSRPAAI QLALKLGVEY REGFIKNRYI GRTFIMPGQG MRKKSVRQKL NAIGSEFKGK
     NVLLVDDSIV RGTTSREIVQ MAREAGARKV FFASAAPPVL FPNVYGIDMP TRDELIAHGR
     TVEEVCAEIT ADRLVYQDID ALKRAISDVN PALTNFEASC FDGIYVTGDV TPAYLDNLET
     ARHNGGKGVS QEDVVRTQLN LNPAVPAE
//
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