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Database: UniProt
Entry: Q22134_CAEEL
LinkDB: Q22134_CAEEL
Original site: Q22134_CAEEL 
ID   Q22134_CAEEL            Unreviewed;       480 AA.
AC   Q22134;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 168.
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   Name=ppat-1 {ECO:0000313|EMBL:CAA84723.1,
GN   ECO:0000313|WormBase:T04A8.5};
GN   ORFNames=CELE_T04A8.5 {ECO:0000313|EMBL:CAA84723.1}, T04A8.5
GN   {ECO:0000313|WormBase:T04A8.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA84723.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CAA84723.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA84723.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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; BX284603; CAA84723.1; -; Genomic_DNA.
DR   PIR; T24422; T24422.
DR   RefSeq; NP_497958.1; NM_065557.6.
DR   AlphaFoldDB; Q22134; -.
DR   SMR; Q22134; -.
DR   STRING; 6239.T04A8.5.1; -.
DR   MEROPS; C44.001; -.
DR   EPD; Q22134; -.
DR   PaxDb; 6239-T04A8-5; -.
DR   PeptideAtlas; Q22134; -.
DR   EnsemblMetazoa; T04A8.5.1; T04A8.5.1; WBGene00011407.
DR   GeneID; 175613; -.
DR   UCSC; T04A8.5; c. elegans.
DR   AGR; WB:WBGene00011407; -.
DR   WormBase; T04A8.5; CE01074; WBGene00011407; ppat-1.
DR   eggNOG; KOG0572; Eukaryota.
DR   GeneTree; ENSGT00970000196077; -.
DR   HOGENOM; CLU_022389_3_1_1; -.
DR   InParanoid; Q22134; -.
DR   OMA; CTHCFDG; -.
DR   OrthoDB; 4975at2759; -.
DR   PhylomeDB; Q22134; -.
DR   Reactome; R-CEL-73817; Purine ribonucleoside monophosphate biosynthesis.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00011407; Expressed in larva and 2 other cell types or tissues.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IBA:GO_Central.
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:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
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   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   1: Evidence at protein level;
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
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   Proteomics identification {ECO:0007829|EPD:Q22134,
KW   ECO:0007829|PeptideAtlas:Q22134};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW   ECO:0000256|PIRNR:PIRNR000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000485}.
FT   DOMAIN          2..245
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         262
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         371
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         372
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         408
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT   BINDING         466
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT   BINDING         469
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
SQ   SEQUENCE   480 AA;  52143 MW;  B4ED8E45F33129DC CRC64;
     MCGIFGIVAA GNYEHLNVLA ANGLAALQHR GTESTGLVGS DGITRDHVEI IKGHGLVRDV
     ITEDNISRMN GQSIIIGHNR YSTAGKKKSG INCVQPFVVY TAMGTVAIAH NGELVDAKQK
     RKEVLHEGVG LSTDTDSELI AQMIAKAIAL NVKCKYGQEM GDITRELAVT MSALNMSYSL
     LVMTFDRLYA IRDPFGNRPL CVGTVYSKNG NPEAFIASSE SCAFPANAKL DFEVRPGEIV
     ELSTGGIKSV WQMKPNTPLA MCIFEYVYFA RNDSEIEGQQ VQTVREECGK TMALEDDLEA
     DIVGNVPDSS LSAAIGYASQ SGITYEPVLH RNSYVGRSFI EPNDEMRQNA IKMKFGVLKK
     KIHGQRIVLV DDSIVRGNTM RTLVKMLRDA GAKEVHLRIA SPPVKFPCFM GINIPTTKEL
     IAAEKTIPEI CQFVGADSVR YLSVDGLVSS VQKGIERAAN FSPGHCTACL TGKYPVAIDL
//
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