ID D1AZ74_SULD5 Unreviewed; 445 AA.
AC D1AZ74;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=Sdel_0174 {ECO:0000313|EMBL:ACZ11212.1};
OS Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurospirillaceae; Sulfurospirillum.
OX NCBI_TaxID=525898 {ECO:0000313|EMBL:ACZ11212.1, ECO:0000313|Proteomes:UP000002222};
RN [1] {ECO:0000313|Proteomes:UP000002222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51133 / DSM 6946 / 5175
RC {ECO:0000313|Proteomes:UP000002222};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Munk A.C., Lu M., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA Hugenholtz P., Woyke T., Wu D., Aumann P., Schneider S., Lang E.,
RA Spring S., Klenk H.P., Eisen J.A.;
RT "The complete genome of Sulfurospirillum deleyianum DSM 6946.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ11212.1, ECO:0000313|Proteomes:UP000002222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51133 / DSM 6946 / 5175
RC {ECO:0000313|Proteomes:UP000002222};
RX PubMed=21304697; DOI=10.4056/sigs.671209;
RA Sikorski J., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D., Goodwin L.,
RA Pitluck S., Ovchinnikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Detter J.C., Han C., Rohde M., Lang E., Spring S., Goker M.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of Sulfurospirillum deleyianum type strain
RT (5175).";
RL Stand. Genomic Sci. 2:149-157(2010).
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 -!- 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|HAMAP-Rule:MF_01931, 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|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01931}.
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DR EMBL; CP001816; ACZ11212.1; -; Genomic_DNA.
DR RefSeq; WP_012855978.1; NC_013512.1.
DR AlphaFoldDB; D1AZ74; -.
DR STRING; 525898.Sdel_0174; -.
DR MEROPS; C44.A01; -.
DR KEGG; sdl:Sdel_0174; -.
DR eggNOG; COG0034; Bacteria.
DR HOGENOM; CLU_022389_3_1_7; -.
DR OrthoDB; 9801213at2; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000002222; Chromosome.
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; 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; IPR000836; PRibTrfase_dom.
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 Pfam; PF00156; Pribosyltran; 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|HAMAP-Rule:MF_01931};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01931};
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|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01931}; Reference proteome {ECO:0000313|Proteomes:UP000002222};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01931,
KW ECO:0000256|PIRNR:PIRNR000485}.
FT DOMAIN 2..221
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-1"
FT BINDING 285
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 347
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 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-2"
SQ SEQUENCE 445 AA; 49436 MW; D70CE7C95F18942C CRC64;
MCAIVGVFDV KHASKIAYYA LFAMQHRGQE ATGISASDGK KIRTLKDNGL VTEVFNEDKL
SFLQGDMAIG HNRYSTAGSD SVRDAQPVAA SYKLGDISIV HNGNLINKHE VRSKLIEQGA
IFQSSMDTEN IIHLIARSQQ GKLQDRIIEA LHIIKGAYCL LIQSRTKMFA MRDRYGVRPL
SIGRFKNGGY IVASETCALD LVDAEFVRDV RPGEMVIFHQ GEKEFESIQL FEPDPHVCAF
EFIYFARPDS VIEGKNVYAI RKKMGMKLAE LAPVEADFVI PVPDSGVSAA LGYAQASGIP
FEMAIVRNHY VGRTFIEPTQ AVRDLKVKLK LSPIHKILEG KKIVVIDDSI VRGTTSRQIV
KLLKRAGAAE VHMRIASPTI EHPCLYGIDT PSYKELISAN KNVEEVREYI EADSLAFLSI
DALKESIGND MNYSLVSFDG NYFIK
//
