ID F9VNF7_SULTO Unreviewed; 403 AA.
AC F9VNF7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=ST1497 {ECO:0000313|EMBL:BAK54603.1};
GN OrderedLocusNames=STK_14970 {ECO:0000313|EMBL:BAK54603.1};
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063 {ECO:0000313|EMBL:BAK54603.1, ECO:0000313|Proteomes:UP000001015};
RN [1] {ECO:0000313|Proteomes:UP000001015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7
RC {ECO:0000313|Proteomes:UP000001015};
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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; BA000023; BAK54603.1; -; Genomic_DNA.
DR RefSeq; WP_010979547.1; NC_003106.2.
DR AlphaFoldDB; F9VNF7; -.
DR STRING; 273063.STK_14970; -.
DR GeneID; 1459533; -.
DR KEGG; sto:STK_14970; -.
DR PATRIC; fig|273063.9.peg.1704; -.
DR eggNOG; arCOG00094; Archaea.
DR OrthoDB; 5976at2157; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
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 InterPro; IPR001763; Rhodanese-like_dom.
DR PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 2.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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|ARBA:ARBA00022842, 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 Reference proteome {ECO:0000313|Proteomes:UP000001015};
KW Transferase {ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:BAK54603.1}.
FT DOMAIN 2..182
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 298..349
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 343
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT BINDING 391
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
FT BINDING 394
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000485-3"
SQ SEQUENCE 403 AA; 44466 MW; 06AFC4599DCC338B CRC64;
MAGIIGVYAF DKIWNISKFL YYGLIGLQNR GYSYSGMSIL KENFQLITNE GAPEDIELPP
NIEGWAGIAY TGTKIGYPII TDFGTLVVDG IIKGDLNEIA KGLYKDPENT LKEINGVFSL
IFLAKDGKML GYRDSYGIKP LEIGGFGFDL AILSSETSGI TVIGGEFRRE IKPGEAVFID
TYEISYSQIN ESRHNYCAID LVYQSRIDSF VFSKNIYEVR VKIGEQLAEE KKIDADVVIG
VPDTAIPFAI GYSKKSGIPY DLGFTRTGSP IRTMLASDDF LKIIGVQLKL NPIKYVVKGK
RVILIDDSMV TGRTLKNTVF ALRSLGAKEV HVLIGSPKLI SKCPYGMEVP EEKDLIAANL
SEEEIAKVIG ADSIYWLSLE GLYKVLGKSI CVGCMTRNYP KVI
//
