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Database: UniProt
Entry: A0A151X620_9HYME
LinkDB: A0A151X620_9HYME
Original site: A0A151X620_9HYME 
ID   A0A151X620_9HYME        Unreviewed;       491 AA.
AC   A0A151X620;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|ARBA:ARBA00033770, ECO:0000256|PIRNR:PIRNR000485};
DE            Short=ATase {ECO:0000256|PIRNR:PIRNR000485};
DE            EC=2.4.2.14 {ECO:0000256|ARBA:ARBA00011941, ECO:0000256|PIRNR:PIRNR000485};
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|ARBA:ARBA00033776, ECO:0000256|PIRNR:PIRNR000485};
GN   ORFNames=ALC60_05293 {ECO:0000313|EMBL:KYQ55794.1};
OS   Trachymyrmex zeteki.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ55794.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ55794.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ55794.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ55794.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex zeteki WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000485-3};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000485-3};
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|PIRNR:PIRNR000485}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00010138,
CC       ECO:0000256|PIRNR:PIRNR000485}.
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DR   EMBL; KQ982490; KYQ55794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151X620; -.
DR   STRING; 64791.A0A151X620; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000075809; Unassembled WGS sequence.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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: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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|PIRNR:PIRNR000485}; Iron {ECO:0000256|PIRSR:PIRSR000485-3};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR000485-3};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000485-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000485-2};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW   ECO:0000256|PIRNR:PIRNR000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:KYQ55794.1}.
FT   DOMAIN          1..250
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   BINDING         269
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT   BINDING         316
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         378
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         379
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         415
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT   BINDING         473
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT   BINDING         476
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
SQ   SEQUENCE   491 AA;  54469 MW;  382FDD44C05782C0 CRC64;
     MYIQERKKYQ LEKTKQFVIF TQSGLVALQH RGQESAGIVT SEGVCSKSFH VHKGMGMINN
     IFNDEIMRKL KGNLGIGHTR YSTSAASEEV NCQPFVVHTA HGALAVGHNG ELVNTESLRK
     MVLGRGVGLS THSDSELITQ ALCLNPPEGE VNGPDWPARI KHLMQLAPLS YSLVIMQRDK
     IYGVRDPYGN RPLCLGKIVP IGNLASRESD DDDDEAEGWV ISSESCGFLS IGARYVREVF
     PGEIVELTRE GIKTIEIVER PNKKRQAFCI FEYVYFARSD SIFEGQMVYS VRMQCGRMLA
     MESPIEADIV SSVPESGTAA AHGYARESKI PFAEVLCKNR YVGRTFIQPS TRLRQLGVAK
     KFGALSENVK GKKIVLIDDS IVRGNTIGPI IKLLRDAGAK EVHIRIASPP LKYPCYMGIN
     IPTREELIAN KLDNVKLAKH VGADSLTYLS VEGLVEAVRY RMDNRESNYI GHCTACLTGE
     YPDELPGDLD W
//
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