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Amidophosphoribosyltransferase (ATase) (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase) (GPATase)

 G2ML75_9ARCH            Unreviewed;       493 AA.
G2ML75;
16-NOV-2011, integrated into UniProtKB/TrEMBL.
16-NOV-2011, sequence version 1.
28-MAR-2018, entry version 45.
RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931};
Short=ATase {ECO:0000256|HAMAP-Rule:MF_01931};
EC=2.4.2.14 {ECO:0000256|HAMAP-Rule:MF_01931};
AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
Short=GPATase {ECO:0000256|HAMAP-Rule:MF_01931};
Name=purF {ECO:0000256|HAMAP-Rule:MF_01931};
ORFNames=Halar_1842 {ECO:0000313|EMBL:AEN05552.1};
halophilic archaeon DL31.
Archaea.
NCBI_TaxID=756883 {ECO:0000313|EMBL:AEN05552.1, ECO:0000313|Proteomes:UP000010096};
[1] {ECO:0000313|EMBL:AEN05552.1, ECO:0000313|Proteomes:UP000010096}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DL31 {ECO:0000313|EMBL:AEN05552.1,
ECO:0000313|Proteomes:UP000010096};
US DOE Joint Genome Institute;
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I.,
Dyall-Smith M., Cavicchioli R., Woyke T.;
"Complete sequence of chromosome of halophilic archaeon DL31.";
Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
phosphoribosylpyrophosphate (PRPP) and glutamine.
{ECO:0000256|HAMAP-Rule:MF_01931}.
-!- CATALYTIC ACTIVITY: 5-phospho-beta-D-ribosylamine + diphosphate +
L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate
+ H(2)O. {ECO:0000256|HAMAP-Rule:MF_01931,
ECO:0000256|PIRNR:PIRNR000485}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01931};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01931};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|HAMAP-Rule:MF_01931,
ECO:0000256|PIRSR:PIRSR000485-3};
Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-3};
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
ribose 1-diphosphate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_01931,
ECO:0000256|PIRNR:PIRNR000485}.
-!- SIMILARITY: In the C-terminal section; belongs to the
purine/pyrimidine phosphoribosyltransferase family.
{ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}.
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EMBL; CP002988; AEN05552.1; -; Genomic_DNA.
ProteinModelPortal; G2ML75; -.
STRING; 756883.Halar_1842; -.
MEROPS; C44.001; -.
EnsemblBacteria; AEN05552; AEN05552; Halar_1842.
KEGG; hah:Halar_1842; -.
eggNOG; arCOG00093; Archaea.
eggNOG; COG0034; LUCA.
KO; K00764; -.
OrthoDB; POG093Z01WR; -.
UniPathway; UPA00074; UER00124.
Proteomes; UP000010096; Chromosome.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
CDD; cd00715; GPATase_N; 1.
CDD; cd06223; PRTases_typeI; 1.
Gene3D; 3.60.20.10; -; 3.
HAMAP; MF_01931; PurF; 1.
InterPro; IPR017932; GATase_2_dom.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000836; PRibTrfase_dom.
InterPro; IPR029057; PRTase-like.
InterPro; IPR005854; PurF.
InterPro; IPR035584; PurF_N.
Pfam; PF00156; Pribosyltran; 1.
PIRSF; PIRSF000485; Amd_phspho_trans; 1.
SUPFAM; SSF53271; SSF53271; 1.
SUPFAM; SSF56235; SSF56235; 1.
TIGRFAMs; TIGR01134; purF; 1.
PROSITE; PS51278; GATASE_TYPE_2; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01931};
Complete proteome {ECO:0000313|Proteomes:UP000010096};
Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931,
ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:AEN05552.1};
Iron {ECO:0000256|HAMAP-Rule:MF_01931};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01931};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01931};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01931};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01931,
ECO:0000256|PIRNR:PIRNR000485};
Reference proteome {ECO:0000313|Proteomes:UP000010096};
Transferase {ECO:0000256|HAMAP-Rule:MF_01931,
ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:AEN05552.1}.
DOMAIN 19 239 Glutamine amidotransferase type-2.
{ECO:0000259|PROSITE:PS51278}.
ACT_SITE 19 19 For GATase activity.
{ECO:0000256|PIRSR:PIRSR000485-1}.
ACT_SITE 19 19 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_01931}.
METAL 257 257 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_01931,
ECO:0000256|PIRSR:PIRSR000485-3}.
METAL 304 304 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01931}.
METAL 372 372 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01931}.
METAL 373 373 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01931}.
METAL 409 409 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_01931,
ECO:0000256|PIRSR:PIRSR000485-3}.
METAL 460 460 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_01931,
ECO:0000256|PIRSR:PIRSR000485-3}.
METAL 463 463 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_01931,
ECO:0000256|PIRSR:PIRSR000485-3}.
SEQUENCE 493 AA; 52526 MW; 69E3C9706AAA2DC2 CRC64;
MDTGPAEGPT GSAGMTEKCG VVGVALEDRG AAHPCYYGLY ALQHRGQESA GIVTHDGFQQ
HDHVEMGLVG EAFDEADIEA LQGSTGVGHV RYPTAGSVDK ACAQPFTVSF RSGSLALSHN
GNLVNANEIR DELAAEGHAF TSDGDTEVIA HDLARNLLDA DLVRAVKRTM ERIHGSYALT
VMHDETVLGV RDPQGNRPLC LGKLDDGYVL ASESAAIDTL GGELIRDVKP GELVLLEPDG
SGYDSYQLIE QPNTAHCFFE HVYFARPDSV IDDSLVYDTR RGLGARLWEE SGVESDVVMP
VPDSGRAFAA GYADAAAADL GDAPEFAEGL MKNRYVGRTF IMPSQDQREQ AVRLKLNPIR
STVEGKSVTL IDDSIVRGTT STQLVALLKE AGAEEVHLRI GAPPIIAPCY MGIDMASREE
LIAAGGDSEA VRAAVNADSL SYLSVDGVAE VLGESRTDLC LGCVTGEYPY DIDGETADRE
VKRPDIDGAL ADD


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