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Database: UniProt
Entry: D4JUX7_9FIRM
LinkDB: D4JUX7_9FIRM
Original site: D4JUX7_9FIRM 
ID   D4JUX7_9FIRM            Unreviewed;       474 AA.
AC   D4JUX7;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011941, 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|PIRNR:PIRNR000485};
GN   ORFNames=EUS_18280 {ECO:0000313|EMBL:CBK96896.1};
OS   [Eubacterium] siraeum 70/3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Oscillospiraceae incertae sedis.
OX   NCBI_TaxID=657319 {ECO:0000313|EMBL:CBK96896.1, ECO:0000313|Proteomes:UP000008803};
RN   [1] {ECO:0000313|EMBL:CBK96896.1, ECO:0000313|Proteomes:UP000008803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70/3 {ECO:0000313|EMBL:CBK96896.1,
RC   ECO:0000313|Proteomes:UP000008803};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Eubacterium siraeum 70/3.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK96896.1, ECO:0000313|Proteomes:UP000008803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70/3 {ECO:0000313|EMBL:CBK96896.1,
RC   ECO:0000313|Proteomes:UP000008803};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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   -!- 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; FP929044; CBK96896.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4JUX7; -.
DR   KEGG; esu:EUS_18280; -.
DR   PATRIC; fig|657319.3.peg.2131; -.
DR   HOGENOM; CLU_022389_4_0_9; -.
DR   BioCyc; ESIR657319:G136K-1549-MONOMER; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000008803; Chromosome.
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:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
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   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   PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF13537; GATase_7; 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|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   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW   ECO:0000256|PIRNR:PIRNR000485};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000485}.
FT   DOMAIN          1..219
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   BINDING         235
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT   BINDING         287
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         350
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         351
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   BINDING         387
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   474 AA;  52888 MW;  99656520CCFB2021 CRC64;
     MGGFFGAASN NDCITDVFFG TDYHSHLGTR RGGMTAYSPD RGFQRAIHSI ENSPFRTKFE
     QDATDMRGKL CIGCISDTDP QPLLVRSKLG IYSICSVGII RNAEQLSTEL LESGCANFET
     MSSGSINSGS LIGALIAQKD NFTEGIRYAQ SKINGTMSLI ILTKDGIIAA RDQYGRLPII
     VGKRSDGYCV SLESFAFQKL GYSTYKELRP GEIDMITADG CEVLSDGDES KMHICSFMWT
     YYGYPNAVYE GVTVETMRTR NGEIMAENDI KNGKLPDVDY VCGIPDSGVP HAIGYANRSG
     IPFARPFIKY TPTWPRSFMP TNQTMRNQVA KMKLIPVHEL IEGKKLLFVD DSIVRGTQMR
     ETVEFLYENG AKEVHMRSAC PPIMYGCKYL NFSRSTSEME LIARQIIDEA EGADGIRFID
     EYSDTNTERG KKLRDEICRR LKLTSLEFQS LDGTVRAIGK PQCELCTYCW NGKE
//
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