ID D0MD77_RHOM4 Unreviewed; 497 AA.
AC D0MD77;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931};
DE Short=ATase {ECO:0000256|HAMAP-Rule:MF_01931};
DE EC=2.4.2.14 {ECO:0000256|HAMAP-Rule:MF_01931};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
DE Short=GPATase {ECO:0000256|HAMAP-Rule:MF_01931};
GN Name=purF {ECO:0000256|HAMAP-Rule:MF_01931};
GN OrderedLocusNames=Rmar_2109 {ECO:0000313|EMBL:ACY48989.1};
OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS obamensis).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC Rhodothermus.
OX NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY48989.1, ECO:0000313|Proteomes:UP000002221};
RN [1] {ECO:0000313|EMBL:ACY48989.1, ECO:0000313|Proteomes:UP000002221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43812 / DSM 4252 / R-10
RC {ECO:0000313|Proteomes:UP000002221};
RX PubMed=21304669; DOI=10.4056/sigs.46736;
RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL Stand. Genomic Sci. 1:283-291(2009).
CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-
CC Rule:MF_01931}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01931,
CC ECO:0000256|PIRSR:PIRSR000485-2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01931,
CC ECO:0000256|PIRSR:PIRSR000485-2};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01931,
CC ECO:0000256|PIRSR:PIRSR000485-3};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01931, 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|HAMAP-Rule:MF_01931,
CC ECO:0000256|PIRNR:PIRNR000485}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01931,
CC ECO:0000256|PIRNR:PIRNR000485}.
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DR EMBL; CP001807; ACY48989.1; -; Genomic_DNA.
DR RefSeq; WP_012844600.1; NC_013501.1.
DR AlphaFoldDB; D0MD77; -.
DR STRING; 518766.Rmar_2109; -.
DR MEROPS; C44.001; -.
DR KEGG; rmr:Rmar_2109; -.
DR eggNOG; COG0034; Bacteria.
DR HOGENOM; CLU_022389_3_3_10; -.
DR OMA; ENAQPTF; -.
DR OrthoDB; 9801213at2; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000002221; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
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 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; 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; 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 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01931};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_01931};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01931};
KW Iron {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-3};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01931,
KW ECO:0000256|PIRSR:PIRSR000485-3};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-
KW 2};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01931,
KW ECO:0000256|PIRSR:PIRSR000485-2};
KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01931,
KW ECO:0000256|PIRNR:PIRNR000485};
KW Reference proteome {ECO:0000313|Proteomes:UP000002221};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01931}.
FT DOMAIN 8..240
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-1"
FT BINDING 261
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-3"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 419
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-3"
FT BINDING 474
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-3"
FT BINDING 477
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-3"
SQ SEQUENCE 497 AA; 55889 MW; 1EF253E95BC7F0A9 CRC64;
MREIKEYCGI FGVYNAPNAA RLIYYGLHAL QHRGQESAGI VTSTYDEVRQ RPVMPVHKGF
GLVLDVFDDP SIFETKLLGR AGIGHNRYST SGSATNPANI QPFVVHYRDG NIALAHNGNL
SNARELRQAF SERGTLFLTT SDSELILHLI AQSRRQRQID QIIDALTQLE GAFSLLILTD
TSLIAVRDPN GFRPLALGRL RNEDGSWAYC VASETCAFDL IGAEYVRDIE PGEILVIDQK
GCETGQFERY FLPRRFRISQ CIFEYVYFAR PDSKVFGEMV DKVRRKLGKQ LAHEAPVPEV
GPDDKPPIVI SVPDSSNTIA LGYTTECQKL GYRCRYEIGL IRNHYVGRTF IAPGQDRREM
RVRCKFNTVE GVLRDRIVVV VDDSIVRGTT SRFLVNMIRQ AGAREVHLRI ASPPVISPCF
YGMDFPSAEE LLANKFASIE EMRRWLGVDS LAYLSVEGLM QAVRSAHPDG LDYCNACFTA
DYPVPVEMGV TKEENEW
//