ID A0A0A2W5B3_BEABA Unreviewed; 505 AA.
AC A0A0A2W5B3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=BBAD15_g178 {ECO:0000313|EMBL:KGQ13872.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ13872.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ13872.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ13872.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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|PIRNR:PIRNR000485};
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 -!- 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}.
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:KGQ13872.1}.
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DR EMBL; ANFO01000017; KGQ13872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2W5B3; -.
DR STRING; 1245745.A0A0A2W5B3; -.
DR HOGENOM; CLU_022389_2_1_1; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
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:0046083; P:adenine metabolic process; IEA:EnsemblFungi.
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};
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:UP000030106};
KW Transferase {ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:KGQ13872.1}.
FT DOMAIN 2..236
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-1"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
SQ SEQUENCE 505 AA; 56659 MW; A78656BE5D4BCD1C CRC64;
MCGIVGIAGF MPVNQSIYDA LTVLQHRGQD AAGIVTIDAL NCFRLRKANG LVSDVFEARH
MQRLQGNMGI GHVRYPTAGS SSASEAQPFY VNSPYGITLA HNGNLTNAHE LRKKLFEEKR
RHINTTSDSE ILLNIFASEL DNFRHYPLEA DNIFAAIAAT NRQIRGAYAC VAMIIGHGMV
AFRDPNGIRP LVIGKRDLGD GRTEYMVASE SVALDTLGFE FLRDIAPGEA VYITEKGQLF
TRQCADNPVS NPCLFEYVYF ARPDSFIDKI SVYSARVEMG KKLGEKIARE WEDLDIDVVI
PIPETSCDIA LEIARILEKP YRQGFVKNRY VGRTFIMPGQ QLRRKSVRRK LNANRAEFRD
KNVLLVDDSI VRGTTSEQII EMAREAGAKK VYLASAAPEI RFPNVYGIDM PSANELIAHG
REVDEIRQII GADGLIFQDL DDLIEAVRVE NPDITQFECS VFNGIYVTKD VDHKYLQYLE
SLRNDDSKAL ARQNEVENLE MHNEG
//
