ID A0A1G2PMF3_TERXR Unreviewed; 477 AA.
AC A0A1G2PMF3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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=A2682_00500 {ECO:0000313|EMBL:OHA49487.1};
OS Terrybacteria sp. (strain RIFCSPHIGHO2_01_FULL_58_15).
OC Bacteria; Candidatus Terrybacteria.
OX NCBI_TaxID=1802363 {ECO:0000313|EMBL:OHA49487.1, ECO:0000313|Proteomes:UP000178690};
RN [1] {ECO:0000313|EMBL:OHA49487.1, ECO:0000313|Proteomes:UP000178690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIFCSPHIGHO2_01_FULL_58_15 {ECO:0000313|Proteomes:UP000178690};
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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=[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}.
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:OHA49487.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MHST01000009; OHA49487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2PMF3; -.
DR STRING; 1802363.A2682_00500; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000178690; 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; 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 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 Metal-binding {ECO:0000256|PIRSR:PIRSR000485-3};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW ECO:0000256|PIRNR:PIRNR000485};
KW Transferase {ECO:0000256|PIRNR:PIRNR000485}.
FT DOMAIN 5..227
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT ACT_SITE 5
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-1"
FT BINDING 245
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT BINDING 395
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT BINDING 457
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT BINDING 460
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
SQ SEQUENCE 477 AA; 52377 MW; 2C59F70F349FDB86 CRC64;
MSIVCGVAGF KGSDEKAALK VAAILAEEQN RGQGSAGIAI HLCGGGDEID VITKRGTVQD
LRMRYDLRDY PGKTAVGVNR YATSGSTRFD MPPLRGEIDG QWMAFGVNGD TVNIDGKPWQ
QYRTSLEAVY HARSDTEVLL HLLAQTEGKD PVERMCRAFP RVEGAFSVVA VLGDGRMVLL
RDRWGFRPLW IGRSEHGVAV ASEDAALRGY QDLREVLPGE IIVIENDLTI AAWQYCPPAE
RLHVCSFESV YLKKSGSRGV NRFRSACGEK LAAELIASRM AETISNHIVV PVLDSGRDAA
LAFAYALGLR VVAGINRSRL SHEMRAFMAE NHDARVAIAE LKHVCDPEVL TGQDVILVED
SLLRGDTLSS IIPVVRRYAR TVRVAIASPP VTGPCYYGIA TPTRNELYAS CHTIEETRRH
IGADSLHYLS LAGYRSCFRH LSIAGYLEEL TPDQHVCDAC MSGNYPPFVP PRHSLPE
//
