(data stored in ACNUC29543 zone)

SWISSPROT: A5GPU8_SYNR3

ID   A5GPU8_SYNR3            Unreviewed;       499 AA.
AC   A5GPU8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 82.
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   ECO:0000313|EMBL:CAK26907.1};
GN   OrderedLocusNames=SynRCC307_0004 {ECO:0000313|EMBL:CAK26907.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK26907.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK26907.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC       phosphoribosylpyrophosphate (PRPP) and glutamine.
CC       {ECO:0000256|HAMAP-Rule:MF_01931}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
CC         = 5-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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-2};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01931, 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;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-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
CC       purine/pyrimidine phosphoribosyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}.
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DR   EMBL; CT978603; CAK26907.1; -; Genomic_DNA.
DR   RefSeq; WP_011934422.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0004; -.
DR   MEROPS; C44.001; -.
DR   EnsemblBacteria; CAK26907; CAK26907; SynRCC307_0004.
DR   KEGG; syr:SynRCC307_0004; -.
DR   eggNOG; ENOG4105CBA; Bacteria.
DR   eggNOG; COG0034; LUCA.
DR   HOGENOM; HOG000033688; -.
DR   KO; K00764; -.
DR   OMA; FRPLCLG; -.
DR   OrthoDB; 267682at2; -.
DR   BioCyc; SSP316278:G1GJL-4-MONOMER; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000001115; 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:0009116; P:nucleoside metabolic process; IEA:InterPro.
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; 3.60.20.10; -; 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; PF13537; GATase_7; 1.
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.
PE   3: Inferred from homology;
DR   PRODOM; A5GPU8.
DR   SWISS-2DPAGE; A5GPU8.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01931};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:CAK26907.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-
KW   3};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRSR:PIRSR000485-3};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRSR:PIRSR000485-2};
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:UP000001115};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01931,
KW   ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:CAK26907.1}.
FT   DOMAIN       26    251       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   ACT_SITE     26     26       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931, ECO:0000256|PIRSR:PIRSR000485-
FT                                1}.
FT   METAL       268    268       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01931, ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
FT   METAL       315    315       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931, ECO:0000256|PIRSR:PIRSR000485-
FT                                2}.
FT   METAL       377    377       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931, ECO:0000256|PIRSR:PIRSR000485-
FT                                2}.
FT   METAL       378    378       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01931, ECO:0000256|PIRSR:PIRSR000485-
FT                                2}.
FT   METAL       414    414       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01931, ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
FT   METAL       465    465       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01931, ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
FT   METAL       468    468       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01931, ECO:0000256|PIRSR:
FT                                PIRSR000485-3}.
SQ   SEQUENCE   499 AA;  54122 MW;  E1A865E3CCA5381C CRC64;
     MKASAAVTIQ WPEQSGGAPD RMEEACGVFG VLASGQQVSS LCYFGLYALQ HRGQEAAGIA
     VFEGDRVRLH KDMGLVSQVF DQDVLERMPG DLAVGHTRYS TTGSSRVCNA QPLVLMTRLG
     PFALAHNGNL VNAMQLRDQL QQQGCQATGT TDSELIAFAV QAQVEAGLDW DEAIKAAARQ
     CQGAFSLVIG TPDALYGLRD GHGLRPLVFG SLPEAEVASW VLSSESCGLD IVGARFHDDV
     AAGELVRFHS GEAQPFRSRW IEETPKLCVF ELIYFARPDS RFFGESLYSY RKRIGQRLAQ
     ESPVEADLVI GVPDSGIPAA IGYSQASGIP FGDGLIKNRY VGRTFIQPTK AMREAGIRVK
     LNPLPDVLEG QRIVVIDDSI VRGTTSRKLV QAFRDAGASE VHMRISSPPV THPCFYGIDT
     DTQDQLIAAR LKLEEIEAHL GVDSLAYLSR EGMLHCAQEQ SENFCSACFD GNYPIPVEDG
     MRKSKLMLEP AGVAAGLKS
//

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