PUR1_METTH
ID PUR1_METTH Reviewed; 474 AA.
AC O26742;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE Flags: Precursor;
GN Name=purF {ECO:0000255|HAMAP-Rule:MF_01931}; OrderedLocusNames=MTH_646;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01931};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01931};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01931};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01931};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01931};
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:0000255|HAMAP-Rule:MF_01931}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01931}.
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DR EMBL; AE000666; AAB85151.1; -; Genomic_DNA.
DR PIR; H69185; H69185.
DR AlphaFoldDB; O26742; -.
DR SMR; O26742; -.
DR STRING; 187420.MTH_646; -.
DR MEROPS; C44.001; -.
DR EnsemblBacteria; AAB85151; AAB85151; MTH_646.
DR KEGG; mth:MTH_646; -.
DR PATRIC; fig|187420.15.peg.626; -.
DR HOGENOM; CLU_022389_3_1_2; -.
DR OMA; ENAQPTF; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000005223; 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 CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; -; 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 Pfam; PF00156; Pribosyltran; 1.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01134; purF; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Glutamine amidotransferase; Glycosyltransferase; Iron; Iron-sulfur;
KW Magnesium; Metal-binding; Purine biosynthesis; Reference proteome;
KW Transferase.
FT PROPEP 1..10
FT /evidence="ECO:0000250"
FT /id="PRO_0000029275"
FT CHAIN 11..474
FT /note="Amidophosphoribosyltransferase"
FT /id="PRO_0000029276"
FT DOMAIN 11..234
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 250
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 396
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 447
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT BINDING 450
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
SQ SEQUENCE 474 AA; 52660 MW; 16BAF93BBF15A0D2 CRC64;
MLGESEVRDK CGIVGIYSQD KKTGVASQIY YALYALQHRG QESAGISTFN GNDILTHRGM
GLVCDVFNPE KLEELKGNVG IGHVRYSTTG ESRIENSQPF WSEFQGGKIA IAHNGDIINS
MELREELEEE GHNFVSTTDS EVICHLLSRE YDEKPNMIYS IKRVSEQLVG SYSLVVLLNQ
DLYVVRDPVG IKPLAFARKG STQIVASETV AFDVIGAEHV RDVQPGEILH LNRGKSYWVA
NAPNTRRAHC MFEYVYFARP DSVIDGRNVY RVRLNIGEAL YREHPANADV VVPVPDSSIP
AAIGYSRASG IPYGEGLIKN RYVGRTFIMP TQEERETAVK LKMNPIRSEL EGKRIVLIDD
SIVRGTTSRA LIDIIRDAGA EEIHLRIGCP PIKSPCYYGI AMATKKELIA STRNVEEIRR
IIGVDSLGYL SIESLVECIG IKKGFLCTGC LDGDYPTPLP SDISEYEAMR SCSR
