ID Q5NEB9_FRATT Unreviewed; 496 AA.
AC Q5NEB9; A0A0G2RPY0;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 124.
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 ECO:0000313|EMBL:CAG46354.1};
GN OrderedLocusNames=FTT_1721c {ECO:0000313|EMBL:CAG46354.1};
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG46354.1, ECO:0000313|Proteomes:UP000001174};
RN [1] {ECO:0000313|EMBL:CAG46354.1, ECO:0000313|Proteomes:UP000001174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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}.
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DR EMBL; AJ749949; CAG46354.1; -; Genomic_DNA.
DR RefSeq; WP_003022690.1; NZ_CP010290.1.
DR RefSeq; YP_170623.1; NC_006570.2.
DR AlphaFoldDB; Q5NEB9; -.
DR IntAct; Q5NEB9; 1.
DR MEROPS; C44.001; -.
DR DNASU; 3191669; -.
DR EnsemblBacteria; CAG46354; CAG46354; FTT_1721c.
DR GeneID; 39482361; -.
DR KEGG; ftu:FTT_1721c; -.
DR PATRIC; fig|177416.36.peg.1004; -.
DR OrthoDB; 9801213at2; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000001174; Chromosome.
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|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:UP000001174};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01931,
KW ECO:0000256|PIRNR:PIRNR000485}.
FT DOMAIN 2..234
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 303
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 365
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"
SQ SEQUENCE 496 AA; 55349 MW; C3DF42FB82E7695B CRC64;
MCGVIGVAGP DQVSYALFYG LSLLQHRGQD AAGIATMDHG HFFIRKNTGL VSDVFTDEKL
EKSKGNMGIG HVRYPTAGSL GAADSQPFYV NNPHGIVFVH NGNLTNVPEL AQMLHDIERR
HLNTSSDSEL LLNFFACGMN KSKGSATSEA VYKACKFVFE HVKGGYACTA MIANFGLIAF
RDPYGIRPLV LGFKEYDDGE KAYMVASESV ALDISGFKVL RDVEPGEVII ITEDRKVHSK
ICAKNPVLAP CLFEYVYFAR PDSIMNGVSV YQARVDAGKI LSKRIKEAWK DKDIDIVIPV
PETGRASAQE IATALGVEYR EGFVKNRYVG RTFIMPENVD RKNFVRRKLN PIPAEFRDKN
VLLVDDSIVR GTTSKRIIEM IRDLGAKSVY LASVSPAVRY PNVYGIDMPV KSDLIAHGKT
IEEIRQWIGV DGLIYLPLED LKEIIQKQNP KIREFEDSVF SGNYITGDVD DAYLDALEKH
RKELKELEKK YKGFDN
//
